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3NDE

Crystal Structure of BlaC-E166A covalently bound with Cephalotin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AARG79
AHOH663
AARG187
AGLU193
AASP255
ATYR286
A9EP308
AHOH403
AHOH415
AHOH447

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
AARG75
AGLU78
AGLU184
AHOH627

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 9EP A 308
ChainResidue
APO41
ACYS83
ASER84
AILE117
ASER142
AASN186
AGLU193
AARG236
ALYS250
ATHR251
AGLY252
ATHR253
AGLY254
AHOH409
AHOH433
AHOH672

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL
ChainResidueDetails
APHE80-LEU95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Increases nucleophilicity of active site Ser","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site","evidences":[{"source":"PubMed","id":"24023821","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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