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1WNI

Crystal Structure of H2-Proteinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS142
AHIS146
AHIS152
AHOH1011

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMTHELGHNL
ChainResidueDetails
ATHR139-LEU148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS142
AHIS146
AHIS152

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2777746
ChainResidueDetails
AGLN1

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN72

222415

PDB entries from 2024-07-10

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