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6QWA

Crystal structure of KPC-3 complexed with relebactam (16 hour soak)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 301
ChainResidue
ASER275
AGLU276
AALA277
AEOH304
AHOH511
AHOH576

site_idAC2
Number of Residues11
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS234
ATHR235
AGLY236
ATHR237
AMK7305
AJJT306
AHOH439
AHOH552
ASER70
ASER130
ATHR216

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 303
ChainResidue
AGLN205
AVAL208
ALYS212
AALA230
ATRP251
AHOH417
AHOH427
AHOH489

site_idAC4
Number of Residues3
Detailsbinding site for residue EOH A 304
ChainResidue
ATYR274
ASO4301
AHOH727

site_idAC5
Number of Residues18
Detailsbinding site for residue MK7 A 305
ChainResidue
ASER70
ALYS73
ATRP105
ASER130
AASN132
ATHR216
ALYS234
ATHR235
AGLY236
ATHR237
ASO4302
AJJT306
AHOH412
AHOH439
AHOH476
AHOH536
AHOH543
AHOH552

site_idAC6
Number of Residues12
Detailsbinding site for residue JJT A 306
ChainResidue
ASER70
ALYS73
ATRP105
ASER130
AASN132
AGLY236
ATHR237
ASO4302
AMK7305
AHOH412
AHOH476
AHOH536

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000250
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU168

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS234

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PDB entries from 2024-07-10

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