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6Z21

Crystal structure of deacylation mutant KPC-2 (E166Q)

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 GOL A 301
ChainResidue
AGLN205
ALYS212
AALA230
ATRP251
AHOH437
AHOH465

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 302
ChainResidue
AGLY175
AARG266
AHOH410
AHOH444
AHOH447
AHOH569
AARG65
APRO67
APRO174

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 303
ChainResidue
ASER275
AGLU276
AALA277
AHOH404
AHOH453

site_idAC4
Number of Residues8
Detailsbinding site for residue SO4 A 304
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
AGLY236
ATHR237
AHOH521
AHOH574

site_idAC5
Number of Residues10
Detailsbinding site for residue SO4 A 305
ChainResidue
AILE173
AILE173
ATYR241
ATYR241
ALYS270
ALYS270
AHOH407
AHOH407
AHOH454
AHOH454

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 306
ChainResidue
AHIS23
AARG184
APRO226
AALA227
AHOH405

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 307
ChainResidue
AARG61
ATHR254
AGLY255
AHOH600

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 A 308
ChainResidue
ALYS273
AHIS274
AHOH421

site_idAC9
Number of Residues3
Detailsbinding site for residue CL A 309
ChainResidue
AARG220
AHIS274
AGLU276

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 2024-07-24

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