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5A0X

Substrate peptide-bound structure of metalloprotease Zmp1 variant E143AY178F from Clostridium difficile

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1221
ChainResidue
AHIS142
AHIS146
AGLU185
CPRO4

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1221
ChainResidue
BHIS142
BHIS146
BGLU185
DPRO4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000305|PubMed:24303041, ECO:0000305|PubMed:26211609
ChainResidueDetails
AALA143
BALA143

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:26211609
ChainResidueDetails
AHIS142
AHIS146
AGLU185
BHIS142
BHIS146
BGLU185

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339
ChainResidueDetails
APHE178
BPHE178

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Interacts with substrate peptide => ECO:0000269|PubMed:26211609
ChainResidueDetails
AASP135
AHIS142
BASP135
BHIS142

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:26211609
ChainResidueDetails
APHE178
BPHE178

218853

PDB entries from 2024-04-24

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