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Chlorine in PDB 4gta: T. Maritima Fdts with Fad, Dump, and Folinic Acid

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

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

Protein crystallography data

The structure of T. Maritima Fdts with Fad, Dump, and Folinic Acid, PDB code: 4gta 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) 39.00 / 1.50
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.300, 110.300, 121.030, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 17.9

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 1 in 4gta

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


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 Folinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:29.2
occ:0.50
O A:HOH478 3.0 40.1 1.0
N A:TYR96 3.2 24.0 1.0
OH A:TYR130 3.7 27.4 1.0
CA A:SER95 3.8 24.6 1.0
CB A:TYR96 3.9 26.1 1.0
C A:SER95 4.0 22.8 1.0
CA A:TYR96 4.1 24.2 1.0
CB A:SER95 4.2 25.3 1.0
O A:HOH503 4.3 38.8 1.0
CZ A:TYR130 4.4 25.1 1.0
OG A:SER95 4.5 29.1 1.0
O A:HOH500 4.6 41.4 1.0
O A:LEU94 4.7 26.1 1.0
CE1 A:TYR130 4.9 26.7 1.0
NZ A:LYS93 4.9 45.0 1.0
C A:TYR96 5.0 24.0 1.0
N A:SER95 5.0 24.0 1.0
O A:TYR96 5.0 26.3 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: Sun Jul 21 15:04:35 2024

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