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Zinc in PDB 3n1m: Crystal Structure of Ihhn Bound to BOCFN3

Protein crystallography data

The structure of Crystal Structure of Ihhn Bound to BOCFN3, PDB code: 3n1m was solved by J.M.Kavran, D.J.Leahy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.86 / 1.69
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.533, 62.533, 163.972, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 20.1

Other elements in 3n1m:

The structure of Crystal Structure of Ihhn Bound to BOCFN3 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ihhn Bound to BOCFN3 (pdb code 3n1m). 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 Crystal Structure of Ihhn Bound to BOCFN3, PDB code: 3n1m:

Zinc binding site 1 out of 1 in 3n1m

Go back to Zinc Binding Sites List in 3n1m
Zinc binding site 1 out of 1 in the Crystal Structure of Ihhn Bound to BOCFN3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Ihhn Bound to BOCFN3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn194

b:19.7
occ:1.00
OD1 B:ASP152 1.9 14.9 1.0
O B:HOH12 2.0 18.7 1.0
NE2 B:HIS145 2.0 17.0 1.0
ND1 B:HIS187 2.1 16.5 1.0
CG B:ASP152 2.7 18.2 1.0
OD2 B:ASP152 2.9 20.6 1.0
HB2 B:HIS187 2.9 23.7 1.0
CE1 B:HIS187 3.0 20.7 1.0
CD2 B:HIS145 3.0 17.9 1.0
CE1 B:HIS145 3.0 19.7 1.0
CG B:HIS187 3.1 18.8 1.0
HE1 B:HIS187 3.2 24.7 1.0
HD2 B:HIS145 3.2 21.2 1.0
HE1 B:HIS145 3.3 23.4 1.0
CB B:HIS187 3.5 19.9 1.0
OE2 B:GLU181 3.7 20.6 1.0
HA B:HIS187 3.8 21.6 1.0
HB1 B:ALA150 4.1 22.9 1.0
CB B:ASP152 4.1 16.6 1.0
ND1 B:HIS145 4.1 20.2 1.0
NE2 B:HIS187 4.2 18.5 1.0
CG B:HIS145 4.2 20.6 1.0
HA B:ASP152 4.2 19.1 1.0
CD2 B:HIS187 4.2 17.0 1.0
CA B:HIS187 4.2 18.2 1.0
O B:HOH218 4.2 24.8 1.0
O B:VAL151 4.2 18.1 1.0
HB3 B:HIS187 4.3 23.7 1.0
HE1 B:HIS139 4.4 25.3 1.0
CA B:ASP152 4.5 16.1 1.0
C B:VAL151 4.5 17.3 1.0
N B:ASP152 4.5 16.7 1.0
O B:HOH277 4.5 34.1 1.0
CD B:GLU181 4.6 19.3 1.0
O B:HOH266 4.6 33.0 1.0
HB2 B:ASP152 4.6 19.7 1.0
HB3 B:ASP152 4.6 19.7 1.0
NE2 B:HIS185 4.6 19.9 1.0
HB3 B:ALA150 4.7 22.9 1.0
OE1 B:GLU181 4.7 20.2 1.0
HD2 B:HIS185 4.8 25.2 1.0
ND1 B:HIS139 4.8 22.2 1.0
CE1 B:HIS139 4.8 21.3 1.0
H B:CYS188 4.8 20.8 1.0
CB B:ALA150 4.8 19.2 1.0
H B:ASP152 4.9 19.8 1.0
CD2 B:HIS185 5.0 21.2 1.0

Reference:

J.M.Kavran, M.D.Ward, O.O.Oladosu, S.Mulepati, D.J.Leahy. All Mammalian Hedgehog Proteins Interact with Cell Adhesion Molecule, Down-Regulated By Oncogenes (Cdo) and Brother of Cdo (Boc) in A Conserved Manner. J.Biol.Chem. V. 285 24584 2010.
ISSN: ISSN 0021-9258
PubMed: 20519495
DOI: 10.1074/JBC.M110.131680
Page generated: Wed Dec 16 04:36:28 2020

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