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Potassium in PDB 2bup: T13G Mutant of the Atpase Fragment of Bovine HSC70

Protein crystallography data

The structure of T13G Mutant of the Atpase Fragment of Bovine HSC70, PDB code: 2bup was solved by M.C.Sousa, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 143.350, 64.300, 46.230, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 22.4

Other elements in 2bup:

The structure of T13G Mutant of the Atpase Fragment of Bovine HSC70 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the T13G Mutant of the Atpase Fragment of Bovine HSC70 (pdb code 2bup). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the T13G Mutant of the Atpase Fragment of Bovine HSC70, PDB code: 2bup:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 2bup

Go back to Potassium Binding Sites List in 2bup
Potassium binding site 1 out of 2 in the T13G Mutant of the Atpase Fragment of Bovine HSC70


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of T13G Mutant of the Atpase Fragment of Bovine HSC70 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K490

b:15.6
occ:1.00
O A:TYR15 2.7 11.7 1.0
OD2 A:ASP10 2.8 9.9 1.0
O A:HOH558 2.8 17.0 1.0
O2B A:ATP489 2.9 5.1 0.4
O A:HOH563 3.0 19.0 1.0
O A:HOH562 3.1 10.0 1.0
O2B A:ADP486 3.1 22.4 0.6
O1B A:ATP489 3.2 5.1 0.4
O3B A:ADP486 3.3 22.5 0.6
PB A:ATP489 3.3 2.2 0.4
CG A:ASP10 3.4 9.7 1.0
PB A:ADP486 3.5 22.0 0.6
O3A A:ADP486 3.5 23.1 0.6
OD1 A:ASP10 3.6 8.5 1.0
MG A:MG487 3.7 12.0 1.0
CA A:GLY12 3.7 11.4 1.0
C A:TYR15 3.7 9.7 1.0
O3A A:ATP489 3.8 4.1 0.4
O2A A:ATP489 3.9 2.2 0.4
O1A A:ATP489 4.0 2.2 0.4
PA A:ATP489 4.0 2.2 0.4
PA A:ADP486 4.1 23.0 0.6
O2A A:ADP486 4.2 25.6 0.6
N A:GLY12 4.3 10.6 1.0
CB A:TYR15 4.4 11.0 1.0
CA A:TYR15 4.5 9.8 1.0
N A:TYR15 4.5 10.2 1.0
O A:HOH1102 4.6 11.1 1.0
N A:SER16 4.6 8.4 1.0
O A:ASP366 4.7 9.7 1.0
CB A:ASP10 4.7 7.6 1.0
CA A:SER16 4.7 8.6 1.0
C A:GLY12 4.8 10.7 1.0
O3B A:ATP489 4.8 9.1 0.4
O3 A:PO4488 4.9 10.8 0.6
O A:HOH573 4.9 9.6 1.0
O A:ASP10 4.9 8.8 1.0
O1B A:ADP486 5.0 20.6 0.6

Potassium binding site 2 out of 2 in 2bup

Go back to Potassium Binding Sites List in 2bup
Potassium binding site 2 out of 2 in the T13G Mutant of the Atpase Fragment of Bovine HSC70


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of T13G Mutant of the Atpase Fragment of Bovine HSC70 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K491

b:14.0
occ:1.00
OG1 A:THR204 2.9 11.2 1.0
OD2 A:ASP206 2.9 12.6 1.0
O2 A:PO4488 2.9 8.8 0.6
OD1 A:ASP199 3.1 10.4 1.0
O A:HOH1119 3.2 35.0 0.4
O A:THR204 3.2 9.8 1.0
O A:HOH560 3.3 19.7 1.0
O2G A:ATP489 3.3 13.7 0.4
O A:ASP199 3.4 9.0 1.0
CG A:ASP199 3.4 10.9 1.0
OD2 A:ASP199 3.7 13.2 1.0
C A:THR204 3.7 10.1 1.0
CG A:ASP206 3.9 12.7 1.0
P A:PO4488 3.9 11.1 0.6
N A:GLY201 3.9 9.1 1.0
O A:HOH561 4.0 11.3 1.0
CB A:THR204 4.0 10.7 1.0
C A:ASP199 4.0 8.4 1.0
MG A:MG487 4.0 12.0 1.0
O4 A:PO4488 4.1 12.4 0.6
O1 A:PO4488 4.2 8.0 0.6
CB A:ASP199 4.2 7.5 1.0
N A:ASP206 4.2 9.9 1.0
O A:HOH509 4.3 14.3 1.0
N A:PHE205 4.3 7.6 1.0
CB A:ASP206 4.3 10.0 1.0
CA A:THR204 4.4 9.3 1.0
O A:HOH551 4.5 15.5 1.0
CA A:PHE205 4.5 8.7 1.0
PG A:ATP489 4.5 14.6 0.4
CA A:GLY201 4.5 11.7 1.0
C A:PHE205 4.6 9.2 1.0
N A:LEU200 4.6 7.4 1.0
C A:LEU200 4.7 9.9 1.0
O3G A:ATP489 4.7 14.7 0.4
CA A:LEU200 4.7 9.5 1.0
CA A:ASP199 4.8 7.5 1.0
O A:HOH545 4.8 13.4 0.6
N A:THR204 4.9 8.9 1.0
O2B A:ADP486 4.9 22.4 0.6
OD1 A:ASP206 4.9 12.6 1.0
O2B A:ATP489 4.9 5.1 0.4
CA A:ASP206 4.9 10.5 1.0

Reference:

M.C.Sousa, D.B.Mckay. The Hydroxyl of Threonine 13 of the Bovine 70-kDa Heat Shock Cognate Protein Is Essential For Transducing the Atp-Induced Conformational Change. Biochemistry V. 37 15392 1998.
ISSN: ISSN 0006-2960
PubMed: 9799500
DOI: 10.1021/BI981510X
Page generated: Sun Dec 13 23:09:09 2020

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