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4OLD

Crystal structure of AmpC beta-lactamase in complex with the product form of (6R,7R)-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid

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
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 2UZ A 401
ChainResidue
AGLN120
AHOH764
AHOH765
AHOH766
AHOH767
AHOH768
AHOH769
AHOH771
AHOH775
AHOH776
AVAL121
AVAL211
ASER212
ATYR221
AALA318
ATHR319
AGLY320
AHOH559

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
ASER64
ATYR150
ALYS315
ATHR316
AGLY317
AALA318
AHOH529
AHOH719
AHOH768
AHOH780

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 403
ChainResidue
AHIS186
AHOH670
AHOH731
AHOH736
BLYS290

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 2UZ B 401
ChainResidue
BGLN120
BASN152
BSER212
BTYR221
BALA318
BTHR319
BGLY320
BHOH749
BHOH812
BHOH814

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 402
ChainResidue
BSER64
BTYR150
BLYS315
BTHR316
BGLY317
BALA318
BHOH546
BHOH608
BHOH814

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 Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:6795623
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS315
BLYS315

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PDB entries from 2024-05-01

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