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5EOE

Crystal structure of extended-spectrum beta-lactamase BEL-1 (orthorhombic form)

Replaces:  4MX4
Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CL A 301
ChainResidue
AGLU96
AALA98
APRO99
ALYS102
BHOH759

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 302
ChainResidue
AHIS32
AASN33
AGLN34

site_idAC3
Number of Residues15
Detailsbinding site for residue CIT A 303
ChainResidue
ALYS65
ATYR97
ASER123
AASN125
ATHR209
ALYS227
ATHR228
AGLY229
ASER230
AHOH454
AHOH523
AHOH530
AHOH559
AHOH566
ASER62

site_idAC4
Number of Residues12
Detailsbinding site for residue 1PE A 304
ChainResidue
AARG236
AGLN262
AGLY263
AGLU264
AGLU265
AALA267
ALEU268
AHOH458
AHOH463
AHOH494
AHOH529
AHOH674

site_idAC5
Number of Residues6
Detailsbinding site for residue IPA A 305
ChainResidue
AARG201
AARG202
AILE205
AHOH668
AHOH709
BTHR107

site_idAC6
Number of Residues4
Detailsbinding site for residue MRD A 306
ChainResidue
AGLU23
ATYR52
AARG53
AHOH590

site_idAC7
Number of Residues3
Detailsbinding site for residue CL A 307
ChainResidue
AARG236
AARG266
AHOH506

site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 301
ChainResidue
ALYS197
BSER43
BASN45

site_idAC9
Number of Residues5
Detailsbinding site for residue CL B 302
ChainResidue
AHOH727
BGLU96
BALA98
BPRO99
BLYS102

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 303
ChainResidue
BARG236
BARG266
BHOH489

site_idAD2
Number of Residues13
Detailsbinding site for residue PGE B 304
ChainResidue
BASP90
BALA92
BPHE93
BLEU94
BGLU95
BHOH404
BHOH405
BHOH406
BHOH415
BHOH429
BHOH614
BHOH687
BHOH691

site_idAD3
Number of Residues5
Detailsbinding site for residue IPA B 305
ChainResidue
BTYR52
BARG53
BHOH469
BHOH605
BHOH740

site_idAD4
Number of Residues9
Detailsbinding site for residue EDO B 306
ChainResidue
BGLY149
BASP150
BLYS151
BVAL152
BSER178
BHOH447
BHOH457
BHOH656
BHOH670

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO B 307
ChainResidue
BTHR166
BPRO167
BASN233

site_idAD6
Number of Residues15
Detailsbinding site for residue CIT B 308
ChainResidue
BHOH514
BHOH568
BHOH575
BHOH592
BHOH651
BSER62
BTYR97
BSER123
BASN125
BTHR209
BLYS227
BTHR228
BGLY229
BSER230
BHOH463

site_idAD7
Number of Residues3
Detailsbinding site for residue CL B 309
ChainResidue
BASP90
BSER91
BHOH720

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaMCSTfKlplAALVL
ChainResidueDetails
APHE58-LEU73

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PDB entries from 2024-11-06

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