Chlorine in PDB 6p2k: Crystal Structure of AFV00434, An Ancestral GH74 Enzyme

Protein crystallography data

The structure of Crystal Structure of AFV00434, An Ancestral GH74 Enzyme, PDB code: 6p2k was solved by P.J.Stogios, T.Skarina, G.Arnal, H.Brumer, A.Savchenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.78 / 2.15
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 173.427, 173.427, 173.427, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 20.4

Other elements in 6p2k:

The structure of Crystal Structure of AFV00434, An Ancestral GH74 Enzyme also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of AFV00434, An Ancestral GH74 Enzyme (pdb code 6p2k). 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 AFV00434, An Ancestral GH74 Enzyme, PDB code: 6p2k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6p2k

Go back to Chlorine Binding Sites List in 6p2k
Chlorine binding site 1 out of 2 in the Crystal Structure of AFV00434, An Ancestral GH74 Enzyme


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 AFV00434, An Ancestral GH74 Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl812

b:52.8
occ:1.00
OE2 A:GLU229 3.7 33.1 1.0
O A:HOH1282 4.3 25.7 1.0
CD A:GLU229 4.4 26.7 1.0
OE1 A:GLU229 4.4 26.3 1.0
O A:HOH1753 4.7 54.6 1.0
O A:HOH956 4.9 30.7 1.0

Chlorine binding site 2 out of 2 in 6p2k

Go back to Chlorine Binding Sites List in 6p2k
Chlorine binding site 2 out of 2 in the Crystal Structure of AFV00434, An Ancestral GH74 Enzyme


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 AFV00434, An Ancestral GH74 Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl816

b:67.6
occ:1.00
OH B:TYR708 3.3 31.1 1.0
CB B:HIS710 3.3 48.5 1.0
CE B:LYS693 3.8 42.2 1.0
CA B:HIS710 3.9 38.1 1.0
O B:HIS710 3.9 40.6 1.0
CE2 B:TYR708 4.0 25.9 1.0
CZ B:TYR708 4.1 26.9 1.0
CE B:MET36 4.1 62.9 1.0
CB B:PRO762 4.3 20.7 1.0
CG B:HIS710 4.4 60.0 1.0
O B:PRO762 4.4 24.7 1.0
C B:HIS710 4.4 40.0 1.0
CG B:PRO762 4.5 23.6 1.0
CG B:LYS693 4.7 30.9 1.0
CD2 B:HIS710 4.7 63.1 1.0
NZ B:LYS693 4.8 46.5 1.0
CE2 B:TYR402 4.8 21.1 1.0
CD B:LYS693 4.9 36.1 1.0
CG B:GLN713 4.9 50.5 1.0

Reference:

G.Arnal, P.J.Stogios, J.Asohan, M.A.Attia, T.Skarina, A.H.Viborg, B.Henrissat, A.Savchenko, H.Brumer. Substrate Specificity, Regiospecificity, and Processivity in Glycoside Hydrolase Family 74. J.Biol.Chem. V. 294 13233 2019.
ISSN: ESSN 1083-351X
PubMed: 31324716
DOI: 10.1074/JBC.RA119.009861
Page generated: Sat Dec 12 13:28:33 2020

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