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5K1D

Crystal structure of a class C beta lactamase/compound1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 5GP A 401
ChainResidue
ASER65
AASN340
AILE343
AGLN356
AHOH525
AHOH543
AHOH640
ALEU120
AGLN121
ATYR151
AILE292
ALYS312
ATHR313
AGLY314
ASER315

site_idAC2
Number of Residues5
Detailsbinding site for residue CD A 402
ChainResidue
AASP244
AHIS259
AHOH562
AHOH675
AHOH683

site_idAC3
Number of Residues4
Detailsbinding site for residue CD A 403
ChainResidue
AGLU207
AVAL278
AHIS351
AHOH676

site_idAC4
Number of Residues2
Detailsbinding site for residue CD A 404
ChainResidue
AHIS24
AGLY359

site_idAC5
Number of Residues3
Detailsbinding site for residue CD A 405
ChainResidue
AHIS0
AHIS148
AHOH673

site_idAC6
Number of Residues6
Detailsbinding site for residue CD A 406
ChainResidue
AHIS161
AHOH636
AHOH655
AHOH660
AHOH667
AHOH686

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK
ChainResidueDetails
APHE61-LYS68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10102","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28242658","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K1F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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