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2BMQ

The Crystal Structure of Nitrobenzene Dioxygenase in complex with nitrobenzene

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0019439biological_processobsolete aromatic compound catabolic process
A0044237biological_processcellular metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005515molecular_functionprotein binding
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0019380biological_process3-phenylpropionate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A1441
ChainResidue
AHIS206
AHIS211
AASP360
AHOH2227
AHOH2401

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI B1195
ChainResidue
BHOH2061
BHOH2256
BHIS14
BGLU18
BGLU160
BHOH2060

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B1196
ChainResidue
BHIS56
BEDO1197
BHOH2001
BHOH2017
BHOH2291

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A1440
ChainResidue
ACYS79
AHIS81
AARG82
ACYS99
ATYR101
AHIS102
ATRP104

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NBZ A1442
ChainResidue
AASN199
AVAL207
AASN258
APHE293
ALEU305
AHOH2401

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1443
ChainResidue
ALYS30
AARG35
AASP151
ASER425

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A1444
ChainResidue
ALYS54
AGLU90
APRO184
ALYS186
AEOH1445
AEOH1446
BGLU70
BARG183

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B1197
ChainResidue
ATYR174
BMET2
BASN4
BHIS56
BNI1196
BHOH2001
BHOH2291
BHOH2292
BHOH2293

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1198
ChainResidue
BTYR88
BGLN102
BLEU191
BVAL192
BPHE193
BHOH2294
BHOH2295

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B1199
ChainResidue
APRO47
ASER48
AASP51
AHOH2051
BARG78
BTYR79
BGLN80
BLEU81
BHOH2296

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1200
ChainResidue
BTHR35
BTHR39
BVAL120
BASN122
BVAL123
BHOH2217

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EOH A1445
ChainResidue
ALEU45
AVAL53
APRO183
APRO184
ATYR327
AEDO1444
AHOH2308
BGLU70
BHOH2163

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EOH A1446
ChainResidue
ALYS54
ALYS56
AGLU61
ALYS186
ATRP325
AEDO1444
BGLU149
BHOH2238

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EOH A1447
ChainResidue
AASN5
ALEU6
ASER8
ATHR13
AGLN14
ALYS15
AASP380

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EOH A1448
ChainResidue
BASN111
BHOH2203
AHIS88
AALA89
AHOH2053

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EOH B1201
ChainResidue
BLEU71
BPRO112
BLYS113
BALA146
BARG147
BARG148

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EOH B1202
ChainResidue
BASP46
BARG115
BPHE116
BHOH2234

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGktlvhaeaGNakgfvCgYH
ChainResidueDetails
ACYS79-HIS102

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AHIS206
AASP203

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AHIS102

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PDB entries from 2024-05-01

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