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Calcium in PDB 4mgq: PBXYN10C Cbm Apo

Protein crystallography data

The structure of PBXYN10C Cbm Apo, PDB code: 4mgq was solved by J.R.Chekan, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.83 / 1.68
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 68.683, 68.683, 111.471, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 20.9

Calcium Binding Sites:

The binding sites of Calcium atom in the PBXYN10C Cbm Apo (pdb code 4mgq). 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 PBXYN10C Cbm Apo, PDB code: 4mgq:

Calcium binding site 1 out of 1 in 4mgq

Go back to Calcium Binding Sites List in 4mgq
Calcium binding site 1 out of 1 in the PBXYN10C Cbm Apo


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of PBXYN10C Cbm Apo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:13.7
occ:1.00
O A:HIS152 2.3 9.9 1.0
O A:THR268 2.4 12.8 1.0
O A:HOH722 2.4 16.4 1.0
O A:HOH1058 2.4 16.8 1.0
OE2 A:GLU270 2.4 16.9 1.0
OD1 A:ASP251 2.5 9.6 1.0
OD2 A:ASP251 2.5 10.9 1.0
CG A:ASP251 2.8 9.7 1.0
C A:THR268 3.5 9.7 1.0
C A:HIS152 3.5 12.0 1.0
CD A:GLU270 3.6 18.1 1.0
N A:HIS152 4.0 9.4 1.0
CA A:THR268 4.0 12.5 1.0
CG A:GLU270 4.1 17.6 1.0
CA A:HIS152 4.3 11.1 1.0
O A:HOH742 4.3 19.1 1.0
CB A:ASP251 4.3 8.6 1.0
CB A:THR268 4.3 14.4 1.0
OD1 A:ASP252 4.5 14.1 1.0
O A:HOH822 4.5 25.9 1.0
O A:HOH1062 4.5 22.0 1.0
N A:VAL153 4.6 10.0 1.0
N A:PHE269 4.6 10.9 1.0
OE1 A:GLU270 4.6 14.8 1.0
CA A:VAL153 4.7 9.4 1.0
C A:PHE269 4.8 12.5 1.0
CB A:PHE269 4.8 10.7 1.0
CG1 A:VAL153 4.8 8.7 1.0
N A:GLU270 4.8 13.9 1.0
CB A:HIS152 4.9 11.2 1.0
C A:LYS151 5.0 11.1 1.0
NH2 A:ARG189 5.0 10.7 1.0
CA A:PHE269 5.0 9.7 1.0
CB A:LYS151 5.0 11.0 1.0

Reference:

M.Zhang, J.R.Chekan, D.Dodd, P.Y.Hong, L.Radlinski, V.Revindran, S.K.Nair, R.I.Mackie, I.Cann. Xylan Utilization in Human Gut Commensal Bacteria Is Orchestrated By Unique Modular Organization of Polysaccharide-Degrading Enzymes. Proc.Natl.Acad.Sci.Usa V. 111 E3708 2014.
ISSN: ISSN 0027-8424
PubMed: 25136124
DOI: 10.1073/PNAS.1406156111
Page generated: Sun Jul 14 10:21:58 2024

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