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1YQS

Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016787molecular_functionhydrolase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BSA A 400
ChainResidue
ASER62
AHOH2253
ATYR159
AARG285
AHIS298
ATHR299
AGLY300
ATHR301
ATYR308
ALEU332

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BSA A 401
ChainResidue
AARG99
ATHR116
AASN117
APHE120
ALEU214
ATYR306
ASER326
AASN327
AHOH2085
AHOH2129
AHOH2344

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
AVAL204
AILE205
AGLY207
AHIS209
ALYS346
AHOH2049
AHOH2217
AHOH2223
AHOH2340

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AASP45
AARG50
AHIS209
AASN211
AHOH2021
AHOH2026
AHOH2207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"12215418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12564922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15581896","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12215418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12564922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15581896","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ei5
ChainResidueDetails
AHIS298
ASER62
AASN161
ALYS65
ATYR159

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PDB entries from 2026-01-21

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