Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HDR

AmpC beta-lactamase in complex with 4-Amino-3-hydroxybenzoic 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 Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
ASER64
ATYR150
ATHR316
AALA318
AHOH536

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 4A3 A 501
ChainResidue
AHOH522
AHOH544
AVAL191
AGLU196
ATYR199
AHIS210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 4A3 B 502
ChainResidue
BVAL191
BGLU196
BTYR199
BHIS210
BHOH525
BHOH567

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4A3 A 503
ChainResidue
AGLN120
AASN152
ASER212
ATYR221
ATHR319
AGLY320
AHOH557
AHOH581

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 4A3 B 504
ChainResidue
BPRO140
BTRP142
BALA143
BHOH520

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4A3 B 505
ChainResidue
BGLN120
BASN152
BVAL211
BSER212
BTYR221
BGLY320
BHOH573
BHOH600

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 4A3 A 506
ChainResidue
ALYS239
APRO240
ALEU241
AARG309
BLYS246
BTHR247
BGLN250

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4A3 B 507
ChainResidue
ATHR302
BTYR259
BTRP260
BILE301
BTHR302
BPRO303
BPRO304
BHOH571

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 4A3 A 508
ChainResidue
AALA141
ATRP142
AALA143
AHOH538

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 4A3 A 509
ChainResidue
APRO277
APRO277
AVAL278
APRO280
ATRP354
AASN358
A4A3511

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 4A3 A 510
ChainResidue
AILE48
AGLY206
AHOH653

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 4A3 A 511
ChainResidue
APRO277
AVAL278
AASN279
A4A3509

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4A3 B 512
ChainResidue
ATRP93
AGLU95
ASER128
ASER129
ALEU132
BASN279
BASP281
BASN285

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 4A3 A 513
ChainResidue
AVAL125
ALYS126
APRO213
AGLY214
AALA215
AHOH563

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 4A3 B 514
ChainResidue
AGLY167
ALEU168
ASER169
AGLN172
BTRP354
BGLN355
BASN358

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 4A3 B 515
ChainResidue
BTHR97
BLYS99
BASN102
BTRP188
BASN190
BPRO192

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

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon