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

2ZJ9

X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a Tripeptide Deletion (Gly286 Ser287 Asp288) on the H10 Helix

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1
ChainResidue
AGLN100
AGLN136
AASN137
ATRP138
AGLN139
AHOH468

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IPA A 362
ChainResidue
AGLU272
AHOH556
AARG148
AMET265
ATYR266

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 2
ChainResidue
AHOH443
BGLN100
BGLN136
BASN137
BTRP138
BGLN139

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IPA B 362
ChainResidue
BARG148
BMET265
BTYR266
BGLU272
BHOH510

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

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
AGLU272
ASER64
ALYS315
ATYR150
ALYS67

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
BGLU272
BSER64
BLYS315
BTYR150
BLYS67

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon