Zinc in PDB 7w7h: S Suis Faka-FAKB2 Complex Structure

Protein crystallography data

The structure of S Suis Faka-FAKB2 Complex Structure, PDB code: 7w7h was solved by Y.Shi, N.Zang, N.Lou, Y.Xu, J.Sun, M.Huang, H.Zhang, H.Lu, C.Zhou, Y.Feng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.26 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 107.749, 107.749, 398.999, 90, 90, 90
R / Rfree (%) 18.2 / 22.1

Zinc Binding Sites:

The binding sites of Zinc atom in the S Suis Faka-FAKB2 Complex Structure (pdb code 7w7h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the S Suis Faka-FAKB2 Complex Structure, PDB code: 7w7h:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7w7h

Go back to Zinc Binding Sites List in 7w7h
Zinc binding site 1 out of 2 in the S Suis Faka-FAKB2 Complex Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of S Suis Faka-FAKB2 Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:78.7
occ:1.00
NE2 A:HIS289 1.9 83.1 1.0
NE2 A:HIS226 1.9 84.5 1.0
NE2 A:HIS291 2.0 83.2 1.0
SG A:CYS244 2.4 75.5 1.0
CE1 A:HIS289 2.8 73.7 1.0
CD2 A:HIS291 2.8 75.5 1.0
CE1 A:HIS226 2.9 73.7 1.0
CD2 A:HIS226 3.0 75.9 1.0
CD2 A:HIS289 3.0 77.3 1.0
CE1 A:HIS291 3.0 73.5 1.0
CB A:CYS244 3.4 69.3 1.0
ND1 A:HIS289 3.9 76.6 1.0
ND1 A:HIS226 4.0 76.8 1.0
CG A:HIS291 4.0 78.0 1.0
CG A:HIS289 4.1 73.5 1.0
ND1 A:HIS291 4.1 74.1 1.0
CG A:HIS226 4.1 77.6 1.0
CA A:CYS244 4.2 68.9 1.0
CG2 A:ILE222 4.5 59.9 1.0
SD A:MET316 4.9 85.0 1.0
C A:CYS244 4.9 77.8 1.0

Zinc binding site 2 out of 2 in 7w7h

Go back to Zinc Binding Sites List in 7w7h
Zinc binding site 2 out of 2 in the S Suis Faka-FAKB2 Complex Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of S Suis Faka-FAKB2 Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:72.7
occ:1.00
NE2 B:HIS291 1.9 76.8 1.0
NE2 B:HIS226 2.0 85.9 1.0
NE2 B:HIS289 2.0 79.5 1.0
SG B:CYS244 2.3 76.2 1.0
CD2 B:HIS291 2.9 72.7 1.0
CE1 B:HIS291 2.9 69.9 1.0
CE1 B:HIS226 2.9 78.5 1.0
CE1 B:HIS289 2.9 73.0 1.0
CD2 B:HIS226 3.0 77.4 1.0
CD2 B:HIS289 3.0 73.3 1.0
CB B:CYS244 3.4 69.4 1.0
ND1 B:HIS291 4.0 71.2 1.0
CG B:HIS291 4.0 72.2 1.0
ND1 B:HIS226 4.0 81.7 1.0
ND1 B:HIS289 4.1 72.5 1.0
CG B:HIS226 4.1 79.9 1.0
CA B:CYS244 4.1 70.7 1.0
CG B:HIS289 4.1 72.9 1.0
CG2 B:ILE222 4.5 61.7 1.0
C B:CYS244 4.9 73.0 1.0
SD B:MET316 5.0 78.0 1.0

Reference:

Y.Shi, N.Zang, N.Lou, Y.Xu, J.Sun, M.Huang, H.Zhang, H.Lu, C.Zhou, Y.Feng. Structure and Mechanism For Streptococcal Fatty Acid Kinase (Fak) System Dedicated to Host Fatty Acid Scavenging. Sci Adv V. 8 Q3944 2022.
ISSN: ESSN 2375-2548
PubMed: 36054360
DOI: 10.1126/SCIADV.ABQ3944
Page generated: Wed Oct 30 13:41:39 2024

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