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7AM5

Crystal structure of Peptiligase mutant - L217H/M222P/A225N

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVLA
ChainResidueDetails
AHIS64-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5249818","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
AASP32electrostatic interaction, electrostatic stabiliser
AHIS64proton acceptor, proton donor
AASN155electrostatic interaction, electrostatic stabiliser
ACYS221nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-12-17

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