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Chlorine in PDB 4gdx: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex

Enzymatic activity of Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex

All present enzymatic activity of Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex:
2.3.2.2; 3.4.19.13; 3.4.19.14;

Protein crystallography data

The structure of Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex, PDB code: 4gdx was solved by M.B.West, Y.Chen, S.Wickham, A.Heroux, K.Cahill, M.H.Hanigan, B.H.M.Mooers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.07 / 1.67
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 105.524, 125.247, 104.468, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 17.4

Other elements in 4gdx:

The structure of Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex (pdb code 4gdx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex, PDB code: 4gdx:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4gdx

Go back to Chlorine Binding Sites List in 4gdx
Chlorine binding site 1 out of 2 in the Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex


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 Human Gamma-Glutamyl Transpeptidase--Glutamate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl606

b:16.1
occ:1.00
HH21 B:ARG409 2.4 22.2 1.0
H A:LEU213 2.4 15.8 0.4
H A:LEU213 2.4 15.8 0.6
H A:GLN212 2.7 18.9 1.0
HB2 A:GLN212 2.8 19.2 1.0
HA A:LEU210 2.9 18.6 1.0
HG11 A:VAL194 3.1 28.7 1.0
O B:HOH1221 3.1 15.6 1.0
HB3 A:LEU210 3.1 15.8 1.0
NH2 B:ARG409 3.2 18.5 1.0
HD2 A:PRO211 3.2 23.7 1.0
N A:LEU213 3.2 13.2 0.6
N A:LEU213 3.3 13.2 0.4
HB2 A:LEU213 3.3 15.8 0.6
HB2 A:LEU213 3.3 16.5 0.4
N A:GLN212 3.3 15.7 1.0
C A:LEU210 3.3 14.1 1.0
HA3 B:GLY414 3.4 13.4 1.0
CA A:LEU210 3.4 15.5 1.0
HG A:LEU213 3.5 15.2 0.4
HD22 A:LEU210 3.5 20.7 1.0
HE B:ARG409 3.5 20.7 1.0
HD23 A:LEU210 3.5 20.7 1.0
HH22 B:ARG409 3.6 22.2 1.0
N A:PRO211 3.6 14.8 1.0
CB A:GLN212 3.7 16.0 1.0
CB A:LEU210 3.7 13.1 1.0
O A:LEU210 3.7 13.8 1.0
HB3 A:LEU213 3.8 15.8 0.6
OE1 A:GLN212 3.8 25.1 1.0
CA A:GLN212 3.8 13.2 1.0
CB A:LEU213 3.9 13.2 0.6
CD A:PRO211 3.9 19.8 1.0
CD2 A:LEU210 3.9 17.3 1.0
HA2 B:GLY414 3.9 13.4 1.0
CB A:LEU213 4.0 13.8 0.4
HD12 A:LEU213 4.0 17.4 0.4
CG1 A:VAL194 4.0 23.9 1.0
C A:GLN212 4.0 12.6 1.0
CG A:LEU213 4.1 12.7 0.4
CA B:GLY414 4.1 11.2 1.0
CZ B:ARG409 4.1 19.3 1.0
NE B:ARG409 4.1 17.3 1.0
CA A:LEU213 4.2 10.5 0.6
HB3 A:GLN212 4.2 19.2 1.0
CA A:LEU213 4.2 10.6 0.4
HG12 A:VAL194 4.3 28.7 1.0
C A:PRO211 4.3 13.9 1.0
HG2 A:PRO211 4.4 30.0 1.0
HG21 A:VAL194 4.4 28.6 1.0
HG13 A:VAL194 4.5 28.7 1.0
CG A:LEU210 4.5 13.8 1.0
HB2 A:LEU210 4.5 15.8 1.0
CA A:PRO211 4.5 17.0 1.0
CD A:GLN212 4.6 30.3 1.0
CD1 A:LEU213 4.6 14.5 0.4
HD3 A:PRO211 4.6 23.7 1.0
H A:ALA214 4.7 14.6 1.0
CG A:GLN212 4.7 20.7 1.0
CG A:PRO211 4.7 25.0 1.0
O B:GLY414 4.7 13.7 1.0
HA A:LEU213 4.7 12.6 0.6
HA A:LEU213 4.7 12.7 0.4
HA A:GLN212 4.8 15.9 1.0
N A:LEU210 4.8 16.8 1.0
HD21 A:LEU210 4.8 20.7 1.0
HB3 A:LEU213 4.8 16.5 0.4
HB A:VAL194 4.9 24.7 1.0
C B:GLY414 4.9 11.0 1.0
CB A:VAL194 5.0 20.6 1.0

Chlorine binding site 2 out of 2 in 4gdx

Go back to Chlorine Binding Sites List in 4gdx
Chlorine binding site 2 out of 2 in the Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1103

b:11.5
occ:1.00
H B:HIS383 2.5 10.6 1.0
HZ3 B:LYS562 2.6 20.1 1.0
HA B:ALA382 2.6 11.0 1.0
HE22 B:GLN545 2.6 14.3 1.0
HB3 A:ASP46 2.9 14.8 1.0
HD3 B:LYS562 2.9 17.8 1.0
OD2 A:ASP46 3.0 13.4 1.0
HB3 B:ALA472 3.1 17.7 1.0
HG11 B:VAL543 3.2 12.8 1.0
NE2 B:GLN545 3.3 11.9 1.0
N B:HIS383 3.3 8.8 1.0
HE21 B:GLN545 3.4 14.3 1.0
HB2 B:ALA472 3.4 17.7 1.0
NZ B:LYS562 3.4 16.7 1.0
CA B:ALA382 3.5 9.1 1.0
CB A:ASP46 3.5 12.3 1.0
HB1 B:ALA382 3.6 13.4 1.0
HB B:VAL543 3.6 12.8 1.0
HB2 A:ASP46 3.6 14.8 1.0
HG12 B:VAL543 3.6 12.8 1.0
CB B:ALA472 3.6 14.7 1.0
CD B:LYS562 3.7 14.8 1.0
HZ2 B:LYS562 3.7 20.1 1.0
CG A:ASP46 3.7 13.3 1.0
CG1 B:VAL543 3.8 10.6 1.0
HD2 B:LYS562 3.8 17.8 1.0
C B:ALA382 3.9 11.0 1.0
CB B:ALA382 3.9 11.2 1.0
CE B:LYS562 4.0 13.3 1.0
HB1 B:ALA472 4.0 17.7 1.0
HZ1 B:LYS562 4.0 20.1 1.0
HE2 B:LYS562 4.0 16.0 1.0
HB2 B:ALA382 4.1 13.4 1.0
O B:HIS383 4.1 9.5 1.0
CB B:VAL543 4.2 10.7 1.0
O B:THR381 4.2 11.2 0.4
O B:THR381 4.4 11.1 0.6
HB3 B:HIS383 4.4 13.2 1.0
CA B:HIS383 4.4 8.0 1.0
O B:HOH1205 4.4 12.3 1.0
HG21 B:VAL543 4.4 14.4 1.0
CD B:GLN545 4.4 10.1 1.0
N B:ALA382 4.6 9.5 1.0
HG13 B:VAL543 4.6 12.8 1.0
C B:HIS383 4.7 10.0 1.0
CB B:HIS383 4.8 11.0 1.0
C B:THR381 4.8 9.2 0.4
HB3 B:ALA382 4.8 13.4 1.0
OE1 B:GLN545 4.9 10.7 1.0
H B:ALA472 4.9 12.1 1.0
C B:THR381 4.9 9.2 0.6
HE3 B:LYS562 4.9 16.0 1.0
CG2 B:VAL543 4.9 12.0 1.0
HB3 B:LYS562 4.9 15.1 1.0
OD1 A:ASP46 4.9 13.6 1.0
O B:VAL543 4.9 11.4 1.0
CA A:ASP46 4.9 12.1 1.0
CG B:LYS562 5.0 14.5 1.0
CA B:ALA472 5.0 11.3 1.0

Reference:

M.B.West, Y.Chen, S.Wickham, A.Heroux, K.Cahill, M.H.Hanigan, B.H.Mooers. Novel Insights Into Eukaryotic Gamma-Glutamyltranspeptidase 1 From the Crystal Structure of the Glutamate-Bound Human Enzyme. J.Biol.Chem. V. 288 31902 2013.
ISSN: ISSN 0021-9258
PubMed: 24047895
DOI: 10.1074/JBC.M113.498139
Page generated: Sat Dec 12 10:39:17 2020

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