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Zinc in PDB 3n1o: Crystal Structure of Ihhn

Protein crystallography data

The structure of Crystal Structure of Ihhn, PDB code: 3n1o 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) 30.99 / 2.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.965, 67.965, 243.281, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ihhn (pdb code 3n1o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Ihhn, PDB code: 3n1o:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 3n1o

Go back to Zinc Binding Sites List in 3n1o
Zinc binding site 1 out of 3 in the Crystal Structure of Ihhn


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn194

b:23.2
occ:1.00
OD1 A:ASP152 2.1 15.0 1.0
NE2 A:HIS145 2.1 15.8 1.0
ND1 A:HIS187 2.1 13.1 1.0
CG A:ASP152 2.9 14.3 1.0
OD2 A:ASP152 3.0 17.0 1.0
CE1 A:HIS187 3.1 21.7 1.0
CE1 A:HIS145 3.1 17.2 1.0
CD2 A:HIS145 3.1 17.7 1.0
CG A:HIS187 3.2 17.0 1.0
OE1 A:GLU181 3.3 35.5 1.0
CB A:HIS187 3.5 14.9 1.0
CE1 A:HIS139 4.1 9.8 1.0
ND1 A:HIS145 4.2 18.6 1.0
NE2 A:HIS187 4.2 16.4 1.0
CG A:HIS145 4.2 20.8 1.0
CB A:ASP152 4.3 13.6 1.0
CA A:HIS187 4.3 16.4 1.0
CD2 A:HIS187 4.3 16.0 1.0
O A:VAL151 4.3 13.2 1.0
O A:HOH229 4.4 5.3 1.0
NE2 A:HIS185 4.4 16.8 1.0
CD A:GLU181 4.4 44.9 1.0
ND1 A:HIS139 4.4 20.0 1.0
C A:VAL151 4.6 11.9 1.0
CA A:ASP152 4.7 15.1 1.0
N A:ASP152 4.7 13.9 1.0
OE2 A:GLU181 4.8 63.0 1.0
CD2 A:HIS185 4.9 19.5 1.0

Zinc binding site 2 out of 3 in 3n1o

Go back to Zinc Binding Sites List in 3n1o
Zinc binding site 2 out of 3 in the Crystal Structure of Ihhn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Ihhn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn194

b:24.5
occ:1.00
OD1 B:ASP152 2.1 18.1 1.0
ND1 B:HIS187 2.2 15.0 1.0
NE2 B:HIS145 2.2 19.9 1.0
O B:HOH213 2.3 26.4 1.0
CG B:ASP152 2.7 21.4 1.0
OD2 B:ASP152 2.7 23.9 1.0
CE1 B:HIS187 3.1 16.6 1.0
CD2 B:HIS145 3.1 17.9 1.0
CG B:HIS187 3.2 15.7 1.0
CE1 B:HIS145 3.3 18.5 1.0
CB B:HIS187 3.6 18.9 1.0
OE1 B:GLU181 3.7 36.2 1.0
CE1 B:HIS139 3.9 26.3 1.0
CB B:ASP152 4.1 16.1 1.0
NE2 B:HIS187 4.2 23.9 1.0
CG B:HIS145 4.3 21.3 1.0
CA B:HIS187 4.3 19.3 1.0
CD2 B:HIS187 4.3 17.9 1.0
ND1 B:HIS145 4.3 21.4 1.0
O B:HOH226 4.4 5.3 1.0
ND1 B:HIS139 4.4 26.6 1.0
O B:VAL151 4.5 19.8 1.0
N B:ASP152 4.5 17.8 1.0
C B:VAL151 4.6 18.3 1.0
CA B:ASP152 4.6 12.5 1.0
NE2 B:HIS185 4.7 29.2 1.0
O B:HOH209 4.8 32.0 1.0
NE2 B:HIS139 4.8 22.0 1.0
CD B:GLU181 4.9 49.7 1.0
CD2 B:HIS185 5.0 29.3 1.0

Zinc binding site 3 out of 3 in 3n1o

Go back to Zinc Binding Sites List in 3n1o
Zinc binding site 3 out of 3 in the Crystal Structure of Ihhn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Ihhn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn194

b:31.1
occ:1.00
OD1 C:ASP152 2.0 18.6 1.0
ND1 C:HIS187 2.1 16.2 1.0
NE2 C:HIS145 2.2 26.0 1.0
O C:HOH206 2.4 27.2 1.0
CG C:ASP152 2.8 23.7 1.0
OD2 C:ASP152 2.9 22.1 1.0
CE1 C:HIS187 3.0 15.4 1.0
CE1 C:HIS145 3.2 26.6 1.0
CG C:HIS187 3.2 24.8 1.0
CD2 C:HIS145 3.2 24.7 1.0
CB C:HIS187 3.6 22.2 1.0
O C:HOH199 3.9 22.3 1.0
CE1 C:HIS139 4.1 39.9 1.0
NE2 C:HIS187 4.2 18.2 1.0
CB C:ASP152 4.3 28.6 1.0
CA C:HIS187 4.3 17.7 1.0
CD2 C:HIS187 4.3 21.0 1.0
ND1 C:HIS145 4.3 27.3 1.0
ND1 C:HIS139 4.3 37.6 1.0
CG C:HIS145 4.4 29.9 1.0
NE2 C:HIS185 4.5 32.1 1.0
O C:HOH208 4.5 53.9 1.0
O C:VAL151 4.5 19.5 1.0
C C:VAL151 4.7 21.8 1.0
N C:ASP152 4.7 18.6 1.0
CA C:ASP152 4.7 19.4 1.0
CD2 C:HIS185 4.9 27.8 1.0
CB C:ALA150 5.0 21.8 1.0
NE2 C:HIS139 5.0 32.8 1.0

Reference:

J.M.Kavran, M.D.Ward, O.O.Oladosu, S.Mulepati, D.J.Leahy. All Mammalian Hedgehog Proteins Interact with Cdo and Boc in A Conserved Manner. J.Biol.Chem. 2010.
ISSN: ESSN 1083-351X
PubMed: 20519495
DOI: 10.1074/JBC.M110.131680
Page generated: Sat Sep 26 11:52:30 2020
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