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Chlorine in PDB 3fwk: Crystal Structure of Candida Glabrata Fmn Adenylyltransferase

Enzymatic activity of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase

All present enzymatic activity of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase:
2.7.7.2;

Protein crystallography data

The structure of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase, PDB code: 3fwk was solved by C.Huerta, D.Borek, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.20
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.090, 80.090, 78.089, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 17.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Candida Glabrata Fmn Adenylyltransferase (pdb code 3fwk). 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 Crystal Structure of Candida Glabrata Fmn Adenylyltransferase, PDB code: 3fwk:

Chlorine binding site 1 out of 1 in 3fwk

Go back to Chlorine Binding Sites List in 3fwk
Chlorine binding site 1 out of 1 in the Crystal Structure of Candida Glabrata Fmn Adenylyltransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl305

b:17.1
occ:1.00
OH A:TYR216 2.9 13.6 1.0
O A:HOH439 3.2 19.2 1.0
N A:LEU223 3.2 14.1 1.0
NZ A:LYS65 3.3 15.2 1.0
O A:HOH671 3.4 36.5 1.0
CA A:SER222 3.7 13.7 1.0
O A:HOH549 3.7 27.1 1.0
CZ A:TYR216 3.8 11.5 1.0
CE1 A:TYR216 3.8 11.6 1.0
O A:HOH321 3.9 26.7 1.0
C A:SER222 3.9 14.8 0.4
C A:SER222 4.0 14.7 0.6
CG A:LEU223 4.1 17.3 1.0
CB A:LEU223 4.1 15.2 1.0
CA A:LEU223 4.2 15.2 1.0
O A:THR221 4.2 13.4 1.0
CG A:LYS65 4.3 13.5 1.0
N A:LYS65 4.4 12.0 1.0
CE A:LYS65 4.5 16.1 1.0
OG A:SER222 4.5 19.6 1.0
CD A:LYS65 4.5 14.4 1.0
CA A:GLY64 4.5 12.0 1.0
N A:SER222 4.6 12.4 1.0
CB A:SER222 4.6 16.2 1.0
CD1 A:LEU223 4.6 19.2 1.0
C A:THR221 4.7 11.2 1.0
O A:LEU223 4.8 19.4 1.0
O A:HOH658 4.9 38.6 1.0
C A:LEU223 4.9 15.7 1.0
C A:GLY64 5.0 11.4 1.0

Reference:

C.Huerta, D.Borek, M.Machius, N.V.Grishin, H.Zhang. Structure and Mechanism of A Eukaryotic Fmn Adenylyltransferase. J.Mol.Biol. V. 389 388 2009.
ISSN: ISSN 0022-2836
PubMed: 19375431
DOI: 10.1016/J.JMB.2009.04.022
Page generated: Fri Jul 11 05:16:34 2025

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