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6T35

Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 401
ChainResidue
ASER127
AALA215

site_idAC2
Number of Residues2
Detailsbinding site for residue PEG A 402
ChainResidue
ALYS246
AGLN250

site_idAC3
Number of Residues9
Detailsbinding site for residue M9W A 404
ChainResidue
AALA318
AGLY320
AHOH503
AHOH626
ASER64
AGLN120
ASER212
ATYR221
AGLY317

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN A 405
ChainResidue
AHIS13
AHIS13
AHIS13
ACL408
ACL408
ACL408

site_idAC5
Number of Residues1
Detailsbinding site for residue ZN A 406
ChainResidue
AHIS186

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 407
ChainResidue
AHIS186
AASP229
AHOH620
AHOH638

site_idAC7
Number of Residues6
Detailsbinding site for residue CL A 408
ChainResidue
AHIS13
AHIS13
AHIS13
AZN405
AZN405
AZN405

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201
ChainResidueDetails
ASER64

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
ATYR150
AASN152
AALA318

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PDB entries from 2024-07-24

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