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Calcium 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:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Mopeia Virus Exonuclease Domain Complexed with Calcium (pdb code 5ls4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Mopeia Virus Exonuclease Domain Complexed with Calcium, PDB code: 5ls4:

Calcium binding site 1 out of 1 in 5ls4

Go back to Calcium Binding Sites List in 5ls4
Calcium 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 Calcium with other atoms in the Ca binding site number 1 of Mopeia Virus Exonuclease Domain Complexed with Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:15.1
occ:0.82
OD2 A:ASP534 2.3 12.8 1.0
O A:HOH761 2.4 19.4 1.0
OE2 A:GLU392 2.4 23.5 1.0
OD2 A:ASP390 2.4 13.8 1.0
O A:HOH731 2.4 23.7 1.0
O A:HOH865 2.5 30.6 1.0
CG A:ASP390 3.3 11.3 1.0
OD1 A:ASP390 3.4 14.8 1.0
CG A:ASP534 3.4 12.7 1.0
HB3 A:HIS529 3.4 15.1 1.0
CD A:GLU392 3.6 14.3 1.0
HH22 A:ARG493 3.6 22.4 1.0
HB2 A:ASP534 3.7 11.5 1.0
HB3 A:ASP534 3.8 11.5 1.0
HG2 A:GLU392 3.9 13.0 1.0
HA A:ALA531 3.9 9.7 1.0
CB A:ASP534 3.9 9.6 1.0
O A:ILE391 3.9 9.3 1.0
O A:HOH713 4.1 28.9 1.0
NH2 A:ARG493 4.3 18.6 1.0
CG A:GLU392 4.3 10.9 1.0
HH21 A:ARG493 4.3 22.4 1.0
CB A:HIS529 4.4 12.6 1.0
HD1 A:HIS529 4.4 26.6 1.0
HZ A:PHE538 4.4 11.7 1.0
OD1 A:ASP534 4.4 13.1 1.0
O A:HOH866 4.5 12.2 1.0
HE2 A:PHE538 4.6 11.9 1.0
OE1 A:GLU392 4.6 21.0 1.0
HB2 A:HIS529 4.7 15.1 1.0
CB A:ASP390 4.7 8.2 1.0
O A:CYS530 4.7 9.0 1.0
HG3 A:GLU392 4.7 13.0 1.0
CA A:ALA531 4.8 8.1 1.0
C A:ILE391 4.8 9.5 1.0
ND1 A:HIS529 4.8 22.2 1.0
H A:ILE391 4.8 9.8 1.0
HB3 A:ASP390 4.8 9.9 1.0
O A:HOH970 4.9 34.3 1.0
CG A:HIS529 4.9 14.7 1.0
C A:CYS530 5.0 8.2 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: Mon Jul 15 07:46:49 2024

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