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Chlorine in PDB 4s35: Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5

Enzymatic activity of Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5

All present enzymatic activity of Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5:
2.7.4.9;

Protein crystallography data

The structure of Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5, PDB code: 4s35 was solved by A.Biswas, J.Jeyakanthan, K.Sekar, S.Kuramitsu, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.479, 62.615, 73.577, 90.00, 97.97, 90.00
R / Rfree (%) 14.6 / 17.4

Other elements in 4s35:

The structure of Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5 also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5 (pdb code 4s35). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5, PDB code: 4s35:

Chlorine binding site 1 out of 1 in 4s35

Go back to Chlorine Binding Sites List in 4s35
Chlorine binding site 1 out of 1 in the Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Amppcp and Tmp Bound Crystal Structure of Thymidylate Kinase (AQ_969) From Aquifex Aeolicus VF5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl205

b:19.7
occ:1.00
 ND2 B:ASN114 3.2 7.7 1.0
O B:HOH430 3.4 22.6 1.0
CB B:ASN114 3.5 7.3 1.0
CG B:ASN114 3.9 8.8 1.0
CD1 B:ILE96 3.9 10.0 1.0
CG2 B:VAL92 4.1 9.3 1.0
CB B:VAL92 4.1 8.8 1.0
CG B:LYS111 4.2 13.9 1.0
CA B:LYS111 4.2 8.3 1.0
O B:LYS111 4.3 7.7 1.0
CB B:LYS111 4.4 10.9 1.0
CG1 B:VAL92 4.6 10.3 1.0
OE1 B:GLU166 4.7 41.9 1.0
C B:LYS111 4.7 7.0 1.0
CG1 B:ILE96 4.8 9.3 1.0
O B:HOH402 4.9 26.6 1.0
CG B:GLU115 5.0 13.8 0.5
CA B:ASN114 5.0 7.9 1.0
CD B:LYS111 5.0 19.7 1.0

Reference:

A.Biswas, J.Jeyakanthan, K.Sekar. Structural Studies of A Hyperthermophilic Thymidylate Kinase Enzyme Reveal Conformational Sub-States Along the Reaction Coordinate Febs J. 2017.
ISSN: ISSN 1742-464X
Page generated: Fri Jul 26 01:43:57 2024

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