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Zinc in PDB 5ls4: Mopeia Virus Exonuclease Domain Complexed with Calcium

Protein crystallography data

The structure of Mopeia Virus Exonuclease Domain Complexed with Calcium, PDB code: 5ls4 was solved by E.L.Yekwa, B.Canard, F.Ferron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.52 / 1.47
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 131.962, 37.913, 48.986, 90.00, 104.07, 90.00
R / Rfree (%) 17 / 19.7

Other elements in 5ls4:

The structure of Mopeia Virus Exonuclease Domain Complexed with Calcium also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Mopeia Virus Exonuclease Domain Complexed with Calcium (pdb code 5ls4). 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 Mopeia Virus Exonuclease Domain Complexed with Calcium, PDB code: 5ls4:

Zinc binding site 1 out of 1 in 5ls4

Go back to Zinc Binding Sites List in 5ls4
Zinc binding site 1 out of 1 in the Mopeia Virus Exonuclease Domain Complexed with Calcium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mopeia Virus Exonuclease Domain Complexed with Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:9.3
occ:1.00
OE2 A:GLU400 2.0 8.5 1.0
NE2 A:HIS510 2.1 10.3 1.0
SG A:CYS530 2.3 9.1 1.0
SG A:CYS507 2.3 9.8 1.0
CD A:GLU400 2.9 8.5 1.0
CD2 A:HIS510 3.0 9.2 1.0
HB2 A:CYS530 3.0 10.8 1.0
HD2 A:HIS510 3.1 11.1 1.0
CE1 A:HIS510 3.1 9.8 1.0
CB A:CYS530 3.2 9.0 1.0
OE1 A:GLU400 3.2 8.5 1.0
HB3 A:CYS507 3.2 14.9 1.0
HE2 A:HIS413 3.2 11.3 1.0
CB A:CYS507 3.3 12.4 1.0
HA A:CYS530 3.3 10.0 1.0
HE1 A:HIS510 3.4 11.8 1.0
HB2 A:CYS507 3.5 14.9 1.0
HE1 A:TYR415 3.6 10.5 1.0
CA A:CYS530 3.7 8.3 1.0
HE1 A:HIS413 3.8 12.2 1.0
H A:ALA531 3.9 11.2 1.0
NE2 A:HIS413 3.9 9.4 1.0
HB2 A:MET509 3.9 15.6 1.0
HH A:TYR415 4.0 13.1 1.0
H A:LEU532 4.0 8.4 1.0
HB3 A:CYS530 4.0 10.8 1.0
CG A:HIS510 4.2 9.6 1.0
ND1 A:HIS510 4.2 10.7 1.0
CE1 A:HIS413 4.2 10.2 1.0
N A:ALA531 4.3 9.3 1.0
CG A:GLU400 4.3 8.4 1.0
HB3 A:LEU532 4.3 8.1 1.0
C A:CYS530 4.3 8.2 1.0
HG3 A:GLU400 4.4 10.1 1.0
CE1 A:TYR415 4.5 8.8 1.0
H A:MET509 4.6 13.4 1.0
HG2 A:GLU400 4.7 10.1 1.0
CA A:CYS507 4.7 9.6 1.0
OH A:TYR415 4.8 10.9 1.0
H A:LEU533 4.8 9.2 1.0
N A:LEU532 4.8 7.0 1.0
HD11 A:ILE434 4.9 14.6 1.0
CB A:MET509 4.9 13.0 1.0
HD13 A:LEU533 4.9 11.8 1.0
HD1 A:HIS510 5.0 12.9 1.0

Reference:

E.Yekwa, J.Khourieh, B.Canard, N.Papageorgiou, F.Ferron. Activity Inhibition and Crystal Polymorphism Induced By Active-Site Metal Swapping. Acta Crystallogr D Struct V. 73 641 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28777079
DOI: 10.1107/S205979831700866X
Page generated: Sun Oct 27 21:18:31 2024

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