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Potassium in PDB 2fhj: Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes

Enzymatic activity of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes

All present enzymatic activity of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes:
2.3.1.101;

Protein crystallography data

The structure of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes, PDB code: 2fhj was solved by P.Acharya, E.Warkentin, R.K.Thauer, S.Shima, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 85.000, 74.150, 103.870, 90.00, 113.54, 90.00
R / Rfree (%) 21.9 / 25.6

Potassium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 17;

Binding sites:

The binding sites of Potassium atom in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes (pdb code 2fhj). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 17 binding sites of Potassium where determined in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes, PDB code: 2fhj:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Potassium binding site 1 out of 17 in 2fhj

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Potassium binding site 1 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K312

b:29.1
occ:1.00
 O A:THR162 2.7 37.1 1.0
O A:LEU251 2.8 33.5 1.0
OG1 A:THR161 2.8 38.2 1.0
O A:HOH4272 3.0 35.5 1.0
OE1 A:GLU113 3.4 46.9 1.0
C A:THR162 3.7 36.6 1.0
CD A:GLU113 3.8 46.7 1.0
C A:LEU251 4.0 33.9 1.0
O A:HOH4467 4.0 41.3 1.0
CB A:THR161 4.1 37.4 1.0
OE2 A:GLU113 4.2 50.4 1.0
CG2 A:THR161 4.3 36.3 1.0
O A:HOH4357 4.3 30.6 1.0
N A:THR162 4.3 36.9 1.0
CB A:GLU113 4.4 41.9 1.0
CB A:ASN252 4.5 34.9 1.0
O A:HOH6011 4.5 39.8 1.0
CA A:GLY163 4.5 35.9 1.0
N A:GLY163 4.5 36.8 1.0
O A:GLU113 4.6 40.4 1.0
CA A:ASN252 4.6 34.9 1.0
CG A:GLU113 4.6 42.8 1.0
CA A:THR162 4.6 37.0 1.0
N A:ASN252 4.7 35.1 1.0
CA A:GLU113 4.7 42.0 1.0
CA A:LEU251 5.0 33.2 1.0

Potassium binding site 2 out of 17 in 2fhj

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Potassium binding site 2 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K313

b:27.2
occ:1.00
 O A:ALA100 2.7 20.5 1.0
O A:MET98 2.7 26.0 1.0
O A:VAL97 2.9 26.7 1.0
O A:ALA103 2.9 28.4 1.0
C A:MET98 3.4 27.3 1.0
N A:ALA103 3.6 27.8 1.0
CD1 A:PHE152 3.8 30.5 1.0
C A:ALA103 3.8 28.5 1.0
C A:ALA100 3.8 21.9 1.0
CA A:MET98 3.8 29.4 1.0
N A:ALA100 3.9 25.1 1.0
C A:VAL97 4.0 29.3 1.0
CA A:ALA103 4.0 28.3 1.0
CE1 A:PHE152 4.2 28.1 1.0
N A:THR99 4.3 27.3 1.0
CB A:ALA103 4.3 29.4 1.0
N A:THR102 4.4 21.9 1.0
C A:THR102 4.4 25.8 1.0
CB B:ALA206 4.4 24.5 1.0
CA A:ALA100 4.4 23.8 1.0
N A:MET98 4.4 28.7 1.0
C A:THR99 4.5 25.5 1.0
CG A:PHE152 4.5 28.9 1.0
OE2 A:GLU149 4.6 35.4 1.0
O A:HOH4008 4.6 17.2 1.0
C A:PRO101 4.7 22.1 1.0
CA A:THR99 4.8 26.2 1.0
CA A:THR102 4.8 24.6 1.0
CB A:PHE152 4.8 32.1 1.0
CB A:ALA100 4.9 23.8 1.0
N A:PRO101 4.9 23.3 1.0

Potassium binding site 3 out of 17 in 2fhj

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Potassium binding site 3 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K315

b:25.8
occ:1.00
 O A:HOH6009 2.6 24.8 1.0
O A:ASP57 2.6 30.9 1.0
O A:VAL193 2.7 28.8 1.0
O A:LYS191 2.7 28.8 1.0
O A:ALA196 2.7 31.8 1.0
O A:ILE190 3.2 28.7 1.0
OD2 A:ASP57 3.2 32.4 1.0
C A:LYS191 3.5 30.0 1.0
C A:ASP57 3.5 29.6 1.0
C A:VAL193 3.7 29.6 1.0
CA A:LYS191 3.8 30.9 1.0
CA A:ASP57 3.9 29.5 1.0
C A:ALA196 3.9 30.0 1.0
N A:VAL193 4.0 29.9 1.0
C A:ILE190 4.2 27.4 1.0
O A:HOH8021 4.2 30.1 1.0
CG A:ASP57 4.3 32.2 1.0
O A:HOH4386 4.4 29.7 1.0
CA A:VAL193 4.4 30.4 1.0
N A:GLY192 4.4 29.3 1.0
N A:LYS191 4.5 30.2 1.0
O A:ILE56 4.5 29.5 1.0
N A:ALA196 4.6 28.5 1.0
N A:GLU194 4.6 31.5 1.0
C A:GLY192 4.7 29.5 1.0
CA A:ALA196 4.7 29.2 1.0
N A:CYS58 4.7 29.5 0.3
N A:CYS58 4.7 29.1 0.7
CB A:ASP57 4.7 30.5 1.0
CA A:GLU194 4.8 31.0 1.0
CB A:ALA196 4.9 29.7 1.0
N A:TYR197 4.9 29.6 1.0
CB A:VAL193 4.9 29.9 1.0
CA A:GLY192 4.9 29.6 1.0
O A:HOH4361 5.0 32.7 1.0

Potassium binding site 4 out of 17 in 2fhj

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Potassium binding site 4 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K316

b:27.3
occ:1.00
 O B:HOH8049 2.2 33.7 1.0
O A:ALA54 2.7 23.2 1.0
O A:PRO199 2.8 26.3 1.0
OE2 B:GLU39 2.8 35.7 1.0
O A:THR41 3.0 29.9 1.0
O A:GLY44 3.1 27.6 1.0
OE1 B:GLU39 3.1 36.5 1.0
CD B:GLU39 3.3 37.4 1.0
C A:GLY44 3.7 27.9 1.0
C A:ALA54 3.8 25.0 1.0
C A:PRO199 3.8 24.9 1.0
C A:THR41 4.1 28.0 1.0
CA A:PRO199 4.2 26.0 1.0
O A:HOH4250 4.2 40.8 1.0
CA A:GLY44 4.3 27.6 1.0
N A:THR45 4.4 28.0 1.0
N A:GLY44 4.4 28.0 1.0
O B:HOH4133 4.4 24.8 1.0
CA A:GLY55 4.6 25.0 1.0
N A:ALA54 4.6 27.4 1.0
CG2 A:THR45 4.6 26.2 1.0
CA A:THR45 4.6 28.3 1.0
N A:GLY55 4.6 25.9 1.0
CA A:ALA54 4.6 27.0 1.0
CB A:PRO199 4.7 26.3 1.0
CB A:THR41 4.7 27.0 1.0
CG B:GLU39 4.7 33.8 1.0
CA A:GLY42 4.8 29.0 1.0
N A:GLY42 4.9 28.9 1.0
O A:HOH4305 4.9 21.8 1.0
OG1 A:THR41 4.9 26.7 1.0
CB A:ALA54 4.9 26.5 1.0
N A:PHE200 4.9 22.8 1.0
CA A:THR41 5.0 27.1 1.0

Potassium binding site 5 out of 17 in 2fhj

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Potassium binding site 5 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K317

b:30.3
occ:1.00
 O B:ALA54 2.6 23.6 1.0
O B:PRO199 2.7 26.7 1.0
O B:GLY44 2.9 27.4 1.0
O B:THR41 3.0 30.1 1.0
OE2 A:GLU39 3.0 35.2 1.0
OE1 A:GLU39 3.3 36.3 1.0
CD A:GLU39 3.5 37.3 1.0
C B:GLY44 3.6 27.9 1.0
C B:PRO199 3.7 25.2 1.0
C B:ALA54 3.7 25.1 1.0
CA B:PRO199 4.0 26.0 1.0
C B:THR41 4.2 28.0 1.0
CA B:GLY44 4.3 27.7 1.0
N B:THR45 4.3 27.9 1.0
CA B:GLY55 4.5 25.4 1.0
N B:GLY44 4.5 27.7 1.0
N B:ALA54 4.5 27.8 1.0
N B:GLY55 4.5 25.8 1.0
CA B:THR45 4.5 28.1 1.0
CB B:PRO199 4.5 26.2 1.0
CG2 B:THR45 4.6 26.1 1.0
CA B:ALA54 4.6 27.0 1.0
CB B:THR41 4.8 27.1 1.0
N B:PHE200 4.8 23.2 1.0
CG A:GLU39 4.8 33.9 1.0
CB B:ALA54 4.9 26.4 1.0
O B:HOH4217 4.9 31.3 1.0
CA B:GLY42 4.9 28.9 1.0
OG1 B:THR41 4.9 26.8 1.0
N B:GLY42 5.0 28.6 1.0

Potassium binding site 6 out of 17 in 2fhj

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Potassium binding site 6 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K319

b:38.0
occ:1.00
 O B:ALA196 2.6 31.8 1.0
O B:VAL193 2.7 28.6 1.0
O B:LYS191 2.7 29.1 1.0
O B:ASP57 2.8 30.8 1.0
O B:ILE190 3.1 28.7 1.0
OD2 B:ASP57 3.3 32.4 1.0
C B:LYS191 3.5 30.0 1.0
C B:VAL193 3.6 29.7 1.0
C B:ASP57 3.6 29.7 1.0
C B:ALA196 3.8 29.9 1.0
CA B:LYS191 3.9 30.8 1.0
CA B:ASP57 3.9 29.7 1.0
N B:VAL193 4.0 29.8 1.0
C B:ILE190 4.1 27.6 1.0
CG B:ASP57 4.3 32.6 1.0
CA B:VAL193 4.4 30.3 1.0
N B:ALA196 4.4 28.6 1.0
N B:GLY192 4.5 29.6 1.0
N B:LYS191 4.5 30.4 1.0
O B:ILE56 4.5 29.9 1.0
N B:GLU194 4.5 31.5 1.0
CA B:ALA196 4.5 29.4 1.0
C B:GLY192 4.7 29.5 1.0
CA B:GLU194 4.7 30.9 1.0
CB B:ALA196 4.7 29.8 1.0
CB B:ASP57 4.7 30.6 1.0
N B:CYS58 4.8 31.2 1.0
N B:TYR197 4.8 30.3 1.0
CB B:VAL193 4.8 30.0 1.0
CA B:TYR197 4.9 29.4 1.0
CA B:GLY192 5.0 29.7 1.0

Potassium binding site 7 out of 17 in 2fhj

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Potassium binding site 7 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K322

b:27.2
occ:1.00
 O B:ALA100 2.7 20.2 1.0
O B:ALA103 2.8 28.9 1.0
O B:MET98 2.8 25.7 1.0
O B:VAL97 2.9 26.8 1.0
O B:HOH4455 3.0 31.4 1.0
C B:MET98 3.5 27.3 1.0
N B:ALA103 3.5 27.7 1.0
C B:ALA103 3.7 28.6 1.0
CD1 B:PHE152 3.8 30.7 1.0
C B:ALA100 3.8 21.8 1.0
CA B:MET98 3.9 29.3 1.0
N B:ALA100 3.9 25.0 1.0
CA B:ALA103 4.0 28.3 1.0
C B:VAL97 4.0 29.2 1.0
CE1 B:PHE152 4.2 28.2 1.0
CB B:ALA103 4.3 29.4 1.0
C B:THR102 4.3 25.8 1.0
N B:THR102 4.3 22.0 1.0
N B:THR99 4.4 26.8 1.0
CA B:ALA100 4.4 23.7 1.0
CB A:ALA206 4.4 24.5 1.0
N B:MET98 4.5 28.5 1.0
C B:THR99 4.5 25.4 1.0
CG B:PHE152 4.6 29.2 1.0
OE2 B:GLU149 4.6 35.5 1.0
O B:HOH4014 4.6 22.4 1.0
C B:PRO101 4.7 22.2 1.0
CA B:THR102 4.7 24.4 1.0
CB B:ALA100 4.8 23.7 1.0
N B:PRO101 4.9 23.1 1.0
CA B:THR99 4.9 26.1 1.0
CB B:PHE152 4.9 32.4 1.0
N B:SER104 5.0 28.4 1.0

Potassium binding site 8 out of 17 in 2fhj

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Potassium binding site 8 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K504

b:58.6
occ:1.00
 O B:THR162 2.9 37.2 1.0
OG1 B:THR161 3.0 38.7 1.0
O B:LEU251 3.2 34.1 1.0
OD1 B:ASN252 3.3 36.6 0.5
OE1 B:GLU113 3.4 47.1 1.0
CD B:GLU113 3.7 46.8 1.0
OE2 B:GLU115 3.7 47.2 1.0
OE2 B:GLU113 3.9 50.6 1.0
C B:THR162 4.0 36.7 1.0
CG B:ASN252 4.0 38.4 0.5
CB B:ASN252 4.2 37.4 0.5
C B:LEU251 4.2 34.4 1.0
CB B:THR161 4.3 37.4 1.0
CB B:GLU113 4.4 41.8 1.0
CB B:ASN252 4.5 35.8 0.5
O B:GLU113 4.5 40.4 1.0
N B:THR162 4.5 37.4 1.0
CG2 B:THR161 4.6 36.4 1.0
CG B:GLU113 4.6 42.9 1.0
CA B:GLU113 4.6 42.0 1.0
CA B:ASN252 4.7 37.1 0.5
CA B:ASN252 4.7 35.9 0.5
N B:GLY163 4.8 37.2 1.0
N B:ASN252 4.8 36.3 0.5
CA B:THR162 4.8 37.1 1.0
CA B:GLY163 4.8 36.0 1.0
N B:ASN252 4.9 35.7 0.5
CD B:GLU115 4.9 48.6 1.0

Potassium binding site 9 out of 17 in 2fhj

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Potassium binding site 9 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 9 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K505

b:38.1
occ:1.00
 O B:HOH4291 3.0 25.4 1.0
CA B:GLY69 3.8 23.8 1.0
OE2 C:GLU265 3.9 56.3 1.0
NE2 C:GLN269 4.2 25.4 1.0
CB C:GLU265 4.5 22.9 1.0
O B:PRO63 4.6 28.1 1.0
O B:GLY69 4.6 20.7 1.0
CD C:GLN269 4.7 29.7 1.0
CA B:GLU64 4.7 36.0 1.0
C B:GLY69 4.7 23.4 1.0
CG C:GLN269 4.8 24.7 1.0
O C:HOH4042 4.8 11.6 1.0
N B:GLY69 4.8 26.4 1.0
O C:GLU265 4.9 25.9 1.0

Potassium binding site 10 out of 17 in 2fhj

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Potassium binding site 10 out of 17 in the Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 10 of Crystal Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K303

b:24.2
occ:1.00
 O C:ALA196 2.5 17.3 1.0
O C:VAL193 2.6 25.9 1.0
O C:LYS191 2.8 26.6 1.0
OD2 C:ASP57 2.9 36.7 1.0
O C:ASP57 3.0 30.8 1.0
O C:HOH6062 3.1 34.5 1.0
O C:ILE190 3.1 25.8 1.0
C C:LYS191 3.6 28.8 1.0
C C:VAL193 3.6 24.3 1.0
C C:ALA196 3.7 21.3 1.0
C C:ASP57 3.7 27.2 1.0
N C:VAL193 3.9 24.2 1.0
CA C:ASP57 3.9 27.1 1.0
CA C:LYS191 4.0 29.3 1.0
CG C:ASP57 4.1 30.2 1.0
C C:ILE190 4.2 24.1 1.0
CA C:VAL193 4.2 23.3 1.0
N C:ALA196 4.3 19.4 1.0
O C:HOH6035 4.4 20.6 1.0
CA C:ALA196 4.5 20.1 1.0
N C:GLU194 4.5 24.1 1.0
O C:HOH4065 4.5 30.7 1.0
N C:GLY192 4.5 26.9 1.0
O C:ILE56 4.6 25.5 1.0
N C:LYS191 4.6 28.0 1.0
CB C:ASP57 4.6 26.5 1.0
CB C:VAL193 4.7 23.6 1.0
CA C:GLU194 4.7 23.1 1.0
C C:GLY192 4.7 24.9 1.0
N C:TYR197 4.7 19.6 1.0
CB C:ALA196 4.8 20.2 1.0
N C:CYS58 4.8 27.9 1.0
CA C:TYR197 4.9 21.2 1.0
N C:GLY195 4.9 19.9 1.0

Reference:

P.Acharya, E.Warkentin, U.Ermler, R.K.Thauer, S.Shima. The Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with Its Coenzymes J.Mol.Biol. V. 357 870 2006.
ISSN: ISSN 0022-2836
PubMed: 16466742
DOI: 10.1016/J.JMB.2006.01.015
Page generated: Mon Aug 12 06:22:17 2024

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