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Chlorine in PDB 4gtf: T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate

Enzymatic activity of T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate

All present enzymatic activity of T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate:
2.1.1.148;

Protein crystallography data

The structure of T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate, PDB code: 4gtf 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) 38.82 / 1.77
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 109.810, 109.810, 122.290, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 17.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate (pdb code 4gtf). 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 (H53A Mutant) with Fad, Dump and Folate, PDB code: 4gtf:

Chlorine binding site 1 out of 1 in 4gtf

Go back to Chlorine Binding Sites List in 4gtf
Chlorine binding site 1 out of 1 in the T. Maritima Fdts (H53A Mutant) with Fad, Dump and Folate


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 (H53A Mutant) with Fad, Dump and Folate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:40.2
occ:0.50
N A:TYR96 3.2 29.2 1.0
CA A:SER95 3.8 30.0 1.0
OH A:TYR130 3.8 33.6 1.0
CB A:TYR96 3.9 33.3 1.0
C A:SER95 4.0 27.8 1.0
CA A:TYR96 4.1 28.9 1.0
O A:HOH503 4.2 41.9 1.0
CB A:SER95 4.2 32.0 1.0
OG A:SER95 4.4 34.0 1.0
O A:HOH514 4.6 45.5 1.0
CZ A:TYR130 4.6 31.2 1.0
O A:LEU94 4.8 30.7 1.0
O A:TYR96 4.9 29.2 1.0
C A:TYR96 4.9 28.9 1.0
N A:SER95 5.0 28.9 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: Sat Dec 12 10:40:46 2020

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