Zinc in PDB 7sev: Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein

Enzymatic activity of Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein

All present enzymatic activity of Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein, PDB code: 7sev was solved by L.Chai, P.Zhu, J.Chai, C.Pang, B.Andi, S.Mcsweeney, J.Shanklin, Q.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.03 / 2.30
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.5, 67.5, 85.212, 90, 90, 90
R / Rfree (%) 20.4 / 24.3

Other elements in 7sev:

The structure of Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein also contains other interesting chemical elements:

Potassium (K) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein (pdb code 7sev). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein, PDB code: 7sev:

Zinc binding site 1 out of 1 in 7sev

Go back to Zinc Binding Sites List in 7sev
Zinc binding site 1 out of 1 in the Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of E Coli Contaminant Protein Yadf Co-Purified with A Plant Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:27.8
occ:1.00
 OD2 A:ASP44 2.0 29.1 1.0
NE2 A:HIS98 2.3 30.1 1.0
SG A:CYS42 2.3 29.0 1.0
SG A:CYS101 2.3 30.1 1.0
CE1 A:HIS98 2.9 29.7 1.0
CG A:ASP44 2.9 30.7 1.0
CB A:ASP44 3.2 29.7 1.0
CB A:CYS42 3.3 27.9 1.0
CB A:CYS101 3.3 27.6 1.0
CD2 A:HIS98 3.4 31.5 1.0
CA A:CYS101 3.7 31.4 1.0
N A:GLY102 4.0 33.5 1.0
ND1 A:HIS98 4.1 32.3 1.0
OD1 A:ASP44 4.1 30.7 1.0
C A:CYS101 4.2 32.9 1.0
O A:HOH431 4.3 28.7 1.0
N A:ASP44 4.3 29.6 1.0
CG A:HIS98 4.3 31.1 1.0
CA A:ASP44 4.4 30.9 1.0
N A:ALA67 4.5 27.0 1.0
N A:GLY103 4.5 29.3 1.0
CA A:ALA67 4.5 26.5 1.0
CA A:CYS42 4.7 27.7 1.0
N A:CYS101 5.0 32.0 1.0

Reference:

L.Chai, P.Zhu, J.Chai, C.Pang, B.Andi, S.Mcsweeney, J.Shanklin, Q.Liu. Alphafold Protein Structure Database For Sequence-Independent Molecular Replacement To Be Published.
Page generated: Wed Oct 30 10:41:49 2024

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