Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4Q8I

Crystal Structure of beta-lactamase from M.tuberculosis covalently complexed with Tebipenem

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 Residues12
DetailsBINDING SITE FOR RESIDUE TEB A 401
ChainResidue
ACYS83
AHOH618
AHOH667
AHOH772
ASER84
ALYS87
ASER142
AGLU182
ATHR232
ATHR251
AGLY252
ATHR253

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AARG79
AARG187
AGLU193
AASP255
ATYR286
AHOH613
AHOH738
AHOH813

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 403
ChainResidue
AARG75
AGLU78
AGLU184
AHOH525
AHOH533
AHOH695
AHOH703
AHOH806

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 404
ChainResidue
APRO216
AASP218
ALYS219
ALYS235
AHOH603
AHOH758

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 405
ChainResidue
AARG140
ATYR141
AHOH590

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

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon