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Potassium in PDB 1ce8: Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp

Enzymatic activity of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp

All present enzymatic activity of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp:
6.3.5.5;

Protein crystallography data

The structure of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp, PDB code: 1ce8 was solved by J.B.Thoden, F.M.Raushel, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 152.100, 163.900, 331.200, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 25.7

Other elements in 1ce8:

The structure of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp also contains other interesting chemical elements:

Manganese (Mn) 12 atoms
Chlorine (Cl) 12 atoms

Potassium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Potassium atom in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp (pdb code 1ce8). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 28 binding sites of Potassium where determined in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp, PDB code: 1ce8:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Potassium binding site 1 out of 28 in 1ce8

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Potassium binding site 1 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5003

b:22.7
occ:1.00
 OE1 A:GLU215 2.5 26.7 1.0
O A:ILE242 2.6 25.7 1.0
OG A:SER247 2.7 22.0 1.0
O A:ASP238 2.8 21.8 1.0
OD1 A:ASN236 2.8 22.4 1.0
O A:ALA239 2.9 20.7 1.0
C A:ALA239 3.5 28.5 1.0
C A:ASP238 3.6 15.6 1.0
CD A:GLU215 3.6 25.1 1.0
CG A:ASN236 3.7 23.8 1.0
CB A:SER247 3.7 8.4 1.0
C A:ILE242 3.8 29.8 1.0
CB A:ASN236 3.9 22.0 1.0
CB A:GLU215 4.0 23.0 1.0
CG A:GLU215 4.1 17.1 1.0
N A:MET240 4.2 18.5 1.0
N A:ALA239 4.2 13.1 1.0
CA A:ALA239 4.3 12.3 1.0
CB A:ASP238 4.3 14.5 1.0
CB A:ILE242 4.3 19.7 1.0
O2' A:ADP5000 4.3 27.7 1.0
N A:ILE242 4.3 20.2 1.0
CA A:ILE242 4.4 30.3 1.0
O A:HIS243 4.4 24.7 1.0
CA A:ASP238 4.4 15.5 1.0
C A:HIS243 4.4 21.6 1.0
N A:THR244 4.5 26.3 1.0
CA A:MET240 4.5 14.7 1.0
OE2 A:GLU215 4.5 32.8 1.0
CA A:THR244 4.5 17.1 1.0
CG2 A:ILE242 4.7 13.5 1.0
CG2 A:THR244 4.8 24.5 1.0
N A:HIS243 4.8 16.3 1.0
ND2 A:ASN236 4.9 14.5 1.0
N A:ASP238 4.9 25.1 1.0
C A:MET240 5.0 27.2 1.0

Potassium binding site 2 out of 28 in 1ce8

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Potassium binding site 2 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5004

b:25.6
occ:1.00
 O A:MET300 2.6 21.8 1.0
O A:HOH5108 2.7 22.5 1.0
OE1 A:GLU299 2.9 29.1 1.0
OE2 A:GLU127 2.9 37.0 1.0
O A:HOH5623 3.3 33.5 1.0
O A:HOH5624 3.3 44.6 1.0
O A:ALA126 3.4 24.0 1.0
C A:MET300 3.6 16.2 1.0
OD1 A:ASN301 3.6 26.5 1.0
CD A:GLU127 3.6 21.4 1.0
CD A:GLU299 3.8 21.5 1.0
MN A:MN5001 3.8 24.4 1.0
NH1 A:ARG129 4.0 20.8 1.0
OE1 A:GLU127 4.1 20.9 1.0
C A:ALA126 4.2 23.4 1.0
N A:MET300 4.2 27.7 1.0
CG A:ASN301 4.3 29.7 1.0
N A:ASN301 4.3 21.2 1.0
CB A:GLU299 4.4 24.7 1.0
CA A:ASN301 4.4 23.0 1.0
CA A:GLU127 4.4 20.0 1.0
CZ A:ARG129 4.5 25.4 1.0
CA A:MET300 4.5 20.2 1.0
CG A:GLU299 4.6 12.5 1.0
OE2 A:GLU299 4.6 20.6 1.0
N A:GLU127 4.6 25.4 1.0
NH2 A:ARG129 4.6 21.4 1.0
CG A:GLU127 4.6 13.3 1.0
O A:HOH5419 4.7 20.1 1.0
O3B A:ADP5000 4.8 21.7 1.0
CD A:PRO302 4.8 21.6 1.0
CB A:ASN301 4.8 23.3 1.0
CB A:ALA126 4.9 19.1 1.0
O A:HOH5109 4.9 23.3 1.0

Potassium binding site 3 out of 28 in 1ce8

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Potassium binding site 3 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5005

b:36.8
occ:1.00
 O A:HOH5225 2.8 4.8 1.0
O3 A:PO45006 2.9 15.3 1.0
OE1 A:GLU217 2.9 26.1 1.0
OE1 A:GLN285 2.9 23.0 1.0
OG1 A:THR244 3.1 21.7 1.0
OD1 A:ASN283 3.2 76.6 1.0
O A:HOH5197 3.4 20.7 1.0
CD A:GLU217 3.7 72.2 1.0
CD A:GLN285 3.7 32.9 1.0
MN A:MN5002 3.8 23.5 1.0
ND2 A:ASN283 3.8 42.5 1.0
O A:HOH5611 3.8 30.1 1.0
CG A:ASN283 3.9 39.8 1.0
O2 A:PO45006 3.9 20.2 1.0
CG A:GLN285 4.0 13.3 1.0
P A:PO45006 4.0 24.8 1.0
OG A:SER307 4.2 23.2 1.0
ND2 A:ASN301 4.2 32.9 1.0
CB A:THR244 4.2 40.7 1.0
CG A:GLU217 4.4 30.7 1.0
CG2 A:THR244 4.4 24.5 1.0
OE2 A:GLU217 4.5 26.8 1.0
OE2 A:GLU299 4.6 20.6 1.0
NH1 A:ARG306 4.6 23.9 1.0
CB A:SER307 4.7 14.3 1.0
NE2 A:GLN285 4.9 20.7 1.0
O4 A:PO45006 4.9 20.3 1.0
O1 A:PO45006 5.0 18.9 1.0

Potassium binding site 4 out of 28 in 1ce8

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Potassium binding site 4 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5009

b:48.3
occ:1.00
 OE2 A:GLU841 2.5 42.3 1.0
O2B A:ADP5007 2.6 46.9 1.0
OE1 A:GLU841 2.9 83.9 1.0
O3B A:ADP5007 2.9 35.5 1.0
CD A:GLU841 3.0 27.7 1.0
OD1 A:ASN843 3.1 53.8 1.0
PB A:ADP5007 3.4 33.3 1.0
O A:HOH5627 3.7 47.5 1.0
O A:HOH5628 3.7 61.3 1.0
O A:HOH5470 3.9 61.2 1.0
MN A:MN5008 4.0 39.3 1.0
CG A:ASN843 4.0 38.7 1.0
O A:HOH5626 4.0 49.3 1.0
NH2 A:ARG845 4.1 0.0 1.0
O A:HOH5563 4.1 31.7 1.0
ND2 A:ASN843 4.1 53.6 1.0
CG A:GLU841 4.4 27.2 1.0
O3A A:ADP5007 4.5 55.6 1.0
O1B A:ADP5007 4.5 33.2 1.0
O2A A:ADP5007 4.8 49.8 1.0

Potassium binding site 5 out of 28 in 1ce8

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Potassium binding site 5 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5010

b:25.2
occ:1.00
 OE1 A:GLU761 2.6 29.8 1.0
O A:VAL787 2.7 25.1 1.0
ND1 A:HIS781 2.7 22.1 1.0
OG A:SER792 2.7 24.1 1.0
O A:GLU783 2.8 23.6 1.0
O A:GLN784 2.8 29.0 1.0
C A:GLN784 3.5 29.6 1.0
CD A:GLU761 3.5 38.5 1.0
C A:GLU783 3.6 30.1 1.0
CB A:GLU761 3.6 19.1 1.0
CE1 A:HIS781 3.6 27.6 1.0
CG A:HIS781 3.7 21.3 1.0
CB A:SER792 3.7 16.7 1.0
C A:VAL787 3.8 32.0 1.0
CB A:HIS781 3.8 26.4 1.0
N A:ALA785 4.1 26.0 1.0
CB A:VAL787 4.1 22.4 1.0
CG A:GLU761 4.2 31.4 1.0
CB A:GLU783 4.2 18.7 1.0
CA A:ALA785 4.2 25.9 1.0
O2' A:ADP5007 4.3 31.2 1.0
N A:GLN784 4.3 22.3 1.0
CA A:GLN784 4.3 31.2 1.0
OE2 A:GLU761 4.3 31.1 1.0
N A:VAL787 4.4 18.8 1.0
CA A:VAL787 4.4 18.4 1.0
O A:HIS788 4.5 23.5 1.0
CA A:GLU783 4.5 21.8 1.0
C A:HIS788 4.5 36.9 1.0
N A:SER789 4.5 27.3 1.0
CG1 A:VAL787 4.5 15.2 1.0
CA A:SER789 4.6 21.8 1.0
O A:HOH5573 4.6 25.4 1.0
NE2 A:HIS781 4.8 24.8 1.0
C A:ALA785 4.8 27.0 1.0
CD2 A:HIS781 4.9 25.7 1.0
N A:GLY786 4.9 19.5 1.0
CA A:GLU761 4.9 13.8 1.0
N A:HIS788 4.9 23.0 1.0
N A:GLU783 5.0 25.1 1.0

Potassium binding site 6 out of 28 in 1ce8

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Potassium binding site 6 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5015

b:28.6
occ:1.00
 O A:GLY112 2.9 54.1 1.0
O A:ASP84 2.9 37.4 1.0
OG1 A:THR114 3.1 56.4 1.0
O A:HOH5395 3.2 57.4 1.0
O A:HOH5023 3.5 50.5 1.0
C A:ASP84 3.7 28.9 1.0
C A:GLY112 3.9 45.5 1.0
N A:THR114 3.9 23.0 1.0
CA A:ASP84 3.9 30.1 1.0
CB A:ASP84 4.0 44.1 1.0
CB A:THR114 4.1 39.6 1.0
OD1 A:ASP84 4.4 44.2 1.0
CA A:VAL113 4.5 45.6 1.0
N A:VAL113 4.5 36.6 1.0
C A:VAL113 4.6 60.3 1.0
CA A:THR114 4.6 0.0 1.0
CG A:ASP84 4.7 59.1 1.0
CA A:GLY112 4.8 28.0 1.0
N A:ALA85 4.9 50.5 1.0
O A:HOH5024 5.0 59.8 1.0

Potassium binding site 7 out of 28 in 1ce8

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Potassium binding site 7 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K5019

b:27.7
occ:1.00
 O B:ASP112 2.6 20.9 1.0
O B:HIS16 2.8 40.5 1.0
O A:HOH5301 3.1 29.9 1.0
O A:HOH5293 3.4 49.1 1.0
C B:ASP112 3.8 20.0 1.0
C B:HIS16 4.0 25.8 1.0
O A:HOH5506 4.2 35.4 1.0
NH2 A:ARG494 4.2 32.1 1.0
CA B:GLY17 4.2 27.8 1.0
CA B:ILE113 4.4 43.0 1.0
CB B:ASP112 4.4 26.6 1.0
CZ A:ARG494 4.6 29.7 1.0
N B:ILE113 4.6 22.6 1.0
N B:GLY17 4.6 35.0 1.0
O B:HOH5044 4.6 13.5 1.0
O B:HOH5114 4.6 42.9 1.0
CG2 B:ILE113 4.7 25.8 1.0
NH1 A:ARG494 4.8 22.7 1.0
CA B:ASP112 4.8 24.8 1.0

Potassium binding site 8 out of 28 in 1ce8

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Potassium binding site 8 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K5023

b:20.9
occ:1.00
 O C:ASP238 2.4 30.0 1.0
OG C:SER247 2.6 19.8 1.0
O C:ILE242 2.7 21.6 1.0
OE1 C:GLU215 2.8 18.9 1.0
O C:ALA239 2.8 19.9 1.0
OD1 C:ASN236 2.9 32.4 1.0
C C:ASP238 3.4 17.6 1.0
C C:ALA239 3.5 27.0 1.0
CB C:ASN236 3.6 19.9 1.0
CG C:ASN236 3.6 20.2 1.0
CB C:SER247 3.7 15.0 1.0
CD C:GLU215 3.8 26.9 1.0
C C:ILE242 3.8 21.1 1.0
CG C:GLU215 4.0 20.7 1.0
CB C:GLU215 4.1 16.0 1.0
N C:ALA239 4.1 20.5 1.0
CA C:ALA239 4.2 19.4 1.0
N C:MET240 4.3 20.2 1.0
CB C:ASP238 4.3 20.6 1.0
O C:HIS243 4.3 25.0 1.0
O2' C:ADP5020 4.3 20.4 1.0
CA C:ASP238 4.4 16.7 1.0
CB C:ILE242 4.4 11.4 1.0
N C:ILE242 4.4 14.9 1.0
C C:HIS243 4.4 25.1 1.0
CA C:ILE242 4.4 15.9 1.0
N C:THR244 4.5 17.4 1.0
CA C:THR244 4.5 19.9 1.0
CA C:MET240 4.6 24.4 1.0
OE2 C:GLU215 4.8 23.3 1.0
N C:HIS243 4.9 25.7 1.0
N C:ASP238 4.9 18.2 1.0
ND2 C:ASN236 5.0 20.5 1.0
CG2 C:ILE242 5.0 6.4 1.0
N C:GLY241 5.0 22.3 1.0
CG2 C:THR244 5.0 13.3 1.0
CA C:SER247 5.0 16.7 1.0

Potassium binding site 9 out of 28 in 1ce8

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Potassium binding site 9 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 9 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K5024

b:28.1
occ:1.00
 O C:MET300 2.6 18.9 1.0
O C:HOH5663 2.7 44.4 1.0
OE2 C:GLU127 2.8 28.8 1.0
OE1 C:GLU299 2.8 17.4 1.0
O C:HOH5128 2.9 24.6 1.0
O C:HOH5662 3.1 33.1 1.0
OD1 C:ASN301 3.3 19.7 1.0
O C:ALA126 3.4 22.8 1.0
O C:HOH5647 3.6 44.8 1.0
C C:MET300 3.7 18.5 1.0
CD C:GLU127 3.7 34.5 1.0
CD C:GLU299 3.8 29.5 1.0
MN C:MN5021 3.8 22.8 1.0
C C:ALA126 4.1 38.9 1.0
N C:MET300 4.2 25.9 1.0
CG C:ASN301 4.2 26.2 1.0
NH1 C:ARG129 4.2 26.5 1.0
CB C:GLU299 4.3 18.1 1.0
OE1 C:GLU127 4.3 25.1 1.0
CA C:GLU127 4.4 13.8 1.0
N C:ASN301 4.4 17.6 1.0
CA C:ASN301 4.4 23.6 1.0
O C:HOH5436 4.5 24.5 1.0
CG C:GLU299 4.5 7.8 1.0
N C:GLU127 4.6 35.0 1.0
CA C:MET300 4.6 16.9 1.0
CZ C:ARG129 4.6 24.8 1.0
NH2 C:ARG129 4.7 22.7 1.0
CG C:GLU127 4.7 21.1 1.0
O3B C:ADP5020 4.7 19.1 1.0
OE2 C:GLU299 4.8 21.6 1.0
CD C:PRO302 4.8 30.9 1.0
CB C:ASN301 4.9 14.1 1.0
CB C:ALA126 5.0 27.7 1.0

Potassium binding site 10 out of 28 in 1ce8

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Potassium binding site 10 out of 28 in the Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 10 of Carbamoyl Phosphate Synthetase From Escherichis Coli with Complexed with the Allosteric Ligand Imp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K5025

b:30.3
occ:1.00
 OE1 C:GLN285 2.5 18.1 1.0
O3 C:PO45026 2.9 10.6 1.0
O C:HOH5244 3.0 7.2 1.0
OE1 C:GLU217 3.0 26.7 1.0
OD1 C:ASN283 3.3 34.0 1.0
OG1 C:THR244 3.3 21.1 1.0
CD C:GLN285 3.4 15.4 1.0
O C:HOH5216 3.4 24.5 1.0
MN C:MN5022 3.7 23.0 1.0
CD C:GLU217 3.8 54.0 1.0
O2 C:PO45026 3.8 15.6 1.0
CG C:GLN285 3.9 11.2 1.0
CG C:ASN283 3.9 32.4 1.0
ND2 C:ASN283 3.9 32.2 1.0
O C:HOH5629 3.9 25.8 1.0
P C:PO45026 4.0 23.4 1.0
OG C:SER307 4.2 29.9 1.0
ND2 C:ASN301 4.2 23.9 1.0
CB C:THR244 4.2 18.7 1.0
CG2 C:THR244 4.3 13.3 1.0
NE2 C:GLN285 4.4 14.7 1.0
CG C:GLU217 4.5 31.8 1.0
OE2 C:GLU299 4.5 21.6 1.0
OE2 C:GLU217 4.6 27.1 1.0
NH1 C:ARG306 4.7 13.1 1.0
CB C:SER307 4.7 19.1 1.0
O4 C:PO45026 4.8 19.9 1.0

Reference:

J.B.Thoden, F.M.Raushel, G.Wesenberg, H.M.Holden. The Binding of Inosine Monophosphate to Escherichia Coli Carbamoyl Phosphate Synthetase. J.Biol.Chem. V. 274 22502 1999.
ISSN: ISSN 0021-9258
PubMed: 10428826
DOI: 10.1074/JBC.274.32.22502
Page generated: Mon Aug 12 04:15:27 2024

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