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Chlorine in PDB 4xcz: X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf

Enzymatic activity of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf

All present enzymatic activity of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf:
2.1.2.9;

Protein crystallography data

The structure of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf, PDB code: 4xcz was solved by J.B.Thoden, C.R.Woodford, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.90 / 1.50
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.235, 78.235, 151.131, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 21.5

Other elements in 4xcz:

The structure of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf also contains other interesting chemical elements:

Potassium (K) 1 atom
Sodium (Na) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf (pdb code 4xcz). 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 X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf, PDB code: 4xcz:

Chlorine binding site 1 out of 1 in 4xcz

Go back to Chlorine Binding Sites List in 4xcz
Chlorine binding site 1 out of 1 in the X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens in Complex with Tdp-QUI3N and N5-Thf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl410

b:16.4
occ:1.00
NZ A:LYS345 3.0 16.4 1.0
O A:HOH885 3.1 24.2 1.0
ND2 A:ASN386 3.2 19.1 1.0
ND2 A:ASN384 3.4 17.0 1.0
CA A:MET381 3.7 13.4 1.0
CE A:LYS345 3.7 16.9 1.0
CB A:ASN384 3.8 14.4 1.0
CG A:MET381 3.8 12.5 1.0
CD A:LYS345 3.8 15.3 1.0
O A:TYR380 3.9 13.7 1.0
N A:MET381 4.0 12.8 1.0
C A:TYR380 4.0 13.4 1.0
CD2 A:LEU349 4.0 22.8 1.0
CG A:ASN384 4.1 17.2 1.0
CB A:MET381 4.3 14.0 1.0
CG A:ASN386 4.3 17.7 1.0
CB A:ASN386 4.4 18.3 1.0
O A:HOH850 4.5 16.3 1.0
CB A:TYR380 4.6 12.6 1.0
O A:HOH884 4.7 20.4 1.0
C A:MET381 4.8 14.0 1.0
O A:MET381 4.9 14.8 1.0
CA A:TYR380 5.0 12.8 1.0

Reference:

C.R.Woodford, J.B.Thoden, H.M.Holden. New Role For the Ankyrin Repeat Revealed By A Study of the N-Formyltransferase From Providencia Alcalifaciens. Biochemistry V. 54 631 2015.
ISSN: ISSN 0006-2960
PubMed: 25574689
DOI: 10.1021/BI501539A
Page generated: Fri Jul 11 22:51:35 2025

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