Zinc in PDB 1wni: Crystal Structure of H2-Proteinase

All present enzymatic activity of Crystal Structure of H2-Proteinase:
3.4.24.53;

The structure of Crystal Structure of H2-Proteinase, PDB code: 1wni was solved by T.Kumasaka, M.Yamamoto, H.Moriyama, N.Tanaka, M.Sato, Y.Katsube, Y.Yamakawa, T.Omori-Satoh, S.Iwanaga, T.Ueki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.800, 77.800, 82.300, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / n/a

The binding sites of Zinc atom in the Crystal Structure of H2-Proteinase (pdb code 1wni). 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 H2-Proteinase, PDB code: 1wni:

Zinc binding site 1 out of 1 in the Crystal Structure of H2-Proteinase


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 H2-Proteinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn999 b:28.8 occ:1.00 NE2 A:HIS152 2.2 14.1 1.0 NE2 A:HIS146 2.3 12.5 1.0 NE2 A:HIS142 2.4 24.5 1.0 O A:HOH1011 2.4 22.7 1.0 CE1 A:HIS152 3.1 27.3 1.0 CD2 A:HIS146 3.2 12.8 1.0 CD2 A:HIS142 3.2 14.7 1.0 CD2 A:HIS152 3.2 25.0 1.0 CE1 A:HIS146 3.3 18.8 1.0 CE1 A:HIS142 3.4 20.7 1.0 OE1 A:GLU143 4.3 26.1 1.0 ND1 A:HIS152 4.3 28.8 1.0 CG A:HIS152 4.4 21.6 1.0 CG A:HIS146 4.4 13.1 1.0 CG A:HIS142 4.4 22.3 1.0 ND1 A:HIS146 4.4 19.6 1.0 ND1 A:HIS142 4.5 26.3 1.0 OE2 A:GLU143 4.5 19.3 1.0 O A:HOH1047 4.7 29.9 1.0 CD A:GLU143 4.8 15.3 1.0 CE A:MET165 4.9 10.6 1.0

T.Kumasaka, M.Yamamoto, H.Moriyama, N.Tanaka, M.Sato, Y.Katsube, Y.Yamakawa, T.Omori-Satoh, S.Iwanaga, T.Ueki. Crystal Structure of H2-Proteinase From the Venom of Trimeresurus Flavoviridis. J.Biochem. V. 119 49 1996.
ISSN: ISSN 0021-924X
PubMed: 8907175
DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A021215