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1SDE

Toward Better Antibiotics: Crystal Structure Of D-Ala-D-Ala Peptidase inhibited by a novel bicyclic phosphate inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008360biological_processregulation of cell shape
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2PB A 400
ChainResidue
AGLY61
AVAL302
AHOH1115
AHOH1169
AHOH1231
AHOH1471
AHOH1473
ASER62
AASP98
ATYR159
AARG285
AHIS298
ATHR299
AGLY300
ATHR301

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
ASER20
ALYS80
AHIS177
AHOH1027
AHOH1032
AHOH1054
AHOH1195
AHOH1228
AHOH1346
AHOH1459

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:12215418, ECO:0000269|PubMed:12564922, ECO:0000269|PubMed:15581896
ChainResidueDetails
ASER62

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12215418, ECO:0000269|PubMed:12564922, ECO:0000269|PubMed:15581896
ChainResidueDetails
APHE120
ATYR159
AARG285
ATHR299
ASER326

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 2024-05-01

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