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Chlorine in PDB 4gtb: T. Maritima Fdts with Fad, Dump, and Raltitrexed.

Enzymatic activity of T. Maritima Fdts with Fad, Dump, and Raltitrexed.

All present enzymatic activity of T. Maritima Fdts with Fad, Dump, and Raltitrexed.:
2.1.1.148;

Protein crystallography data

The structure of T. Maritima Fdts with Fad, Dump, and Raltitrexed., PDB code: 4gtb was solved by I.I.Mathews, S.A.Lesley, A.Kohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.09 / 1.70
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.570, 110.570, 121.730, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 18.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T. Maritima Fdts with Fad, Dump, and Raltitrexed. (pdb code 4gtb). 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 T. Maritima Fdts with Fad, Dump, and Raltitrexed., PDB code: 4gtb:

Chlorine binding site 1 out of 1 in 4gtb

Go back to Chlorine Binding Sites List in 4gtb
Chlorine binding site 1 out of 1 in the T. Maritima Fdts with Fad, Dump, and Raltitrexed.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T. Maritima Fdts with Fad, Dump, and Raltitrexed. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:32.0
occ:0.50
O A:HOH482 2.9 46.4 1.0
N A:TYR96 3.6 31.8 1.0
CB A:SER95 3.9 32.7 1.0
CA A:SER95 3.9 31.8 1.0
OG A:SER95 4.1 36.4 1.0
O A:HOH464 4.2 43.7 1.0
C A:SER95 4.3 30.4 1.0
CB A:TYR96 4.3 34.3 1.0
CA A:TYR96 4.5 31.8 1.0
O A:TYR96 4.6 31.2 1.0
O A:HOH510 4.9 47.1 1.0
OH A:TYR130 4.9 32.7 1.0
C A:TYR96 4.9 31.2 1.0

Reference:

E.M.Koehn, L.L.Perissinotti, S.Moghram, A.Prabhakar, S.A.Lesley, I.I.Mathews, A.Kohen. Folate Binding Site of Flavin-Dependent Thymidylate Synthase. Proc.Natl.Acad.Sci.Usa V. 109 15722 2012.
ISSN: ISSN 0027-8424
PubMed: 23019356
DOI: 10.1073/PNAS.1206077109
Page generated: Fri Jul 11 15:55:13 2025

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