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Chlorine in PDB 4aqj: Structure of Human S100A7 D24G Bound to Zinc and Calcium

Protein crystallography data

The structure of Structure of Human S100A7 D24G Bound to Zinc and Calcium, PDB code: 4aqj was solved by J.I.Murray, M.L.Tonkin, A.L.Whiting, F.Peng, B.Farnell, F.Hof, M.J.Boulanger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.76 / 1.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 51.480, 51.480, 117.230, 90.00, 90.00, 90.00
R / Rfree (%) 18.901 / 22.532

Other elements in 4aqj:

The structure of Structure of Human S100A7 D24G Bound to Zinc and Calcium also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Human S100A7 D24G Bound to Zinc and Calcium (pdb code 4aqj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Human S100A7 D24G Bound to Zinc and Calcium, PDB code: 4aqj:

Chlorine binding site 1 out of 1 in 4aqj

Go back to Chlorine Binding Sites List in 4aqj
Chlorine binding site 1 out of 1 in the Structure of Human S100A7 D24G Bound to Zinc and Calcium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human S100A7 D24G Bound to Zinc and Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1098

b:25.0
occ:1.00
ZN A:ZN1099 2.2 20.8 1.0
NE2 A:HIS90 3.2 24.1 1.0
CE1 A:HIS90 3.4 26.4 1.0
NE2 A:HIS86 3.6 14.8 1.0
CE1 A:HIS86 4.1 19.6 1.0
CD2 A:HIS90 4.6 21.1 1.0
ND1 A:HIS90 4.7 22.4 1.0
CD2 A:HIS86 4.8 19.6 1.0

Reference:

J.I.Murray, M.L.Tonkin, A.L.Whiting, F.Peng, B.Farnell, J.T.Cullen, F.Hof, M.J.Boulanger. Structural Characterization of S100A15 Reveals A Novel Zinc Coordination Site Among S100 Proteins and Altered Surface Chemistry with Functional Implications For Receptor Binding. Bmc Struct.Biol. V. 12 16 2012.
ISSN: ISSN 1472-6807
PubMed: 22747601
DOI: 10.1186/1472-6807-12-16
Page generated: Sun Jul 21 09:22:39 2024

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