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2N6J

Solution structure of Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficile

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS142
AHIS146
ATYR178
AGLU185
AHOH302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000305|PubMed:24303041, ECO:0000305|PubMed:26211609
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:26211609
ChainResidueDetails
AHIS142
AHIS146
AGLU185

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339
ChainResidueDetails
ATYR178

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Interacts with substrate peptide => ECO:0000269|PubMed:26211609
ChainResidueDetails
AASP135
AHIS142

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:26211609
ChainResidueDetails
ATYR178

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PDB entries from 2024-08-14

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