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3O5A

Crystal Structure of partially reduced Periplasmic Nitrate Reductase from Cupriavidus necator using Ionic Liquids

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0008940molecular_functionnitrate reductase activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0030151molecular_functionmolybdenum ion binding
A0042128biological_processnitrate assimilation
A0042597cellular_componentperiplasmic space
A0043546molecular_functionmolybdopterin cofactor binding
A0045333biological_processcellular respiration
A0046872molecular_functionmetal ion binding
A0050140molecular_functionnitrate reductase (cytochrome) activity
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A1990204cellular_componentoxidoreductase complex
B0009061biological_processanaerobic respiration
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 1801
ChainResidue
ACYS19
APHE21
ACYS22
AGLY25
ACYS26
AASN53
ACYS54
AGLY57
APRO194

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MOS A 1802
ChainResidue
ACYS152
AGLN384
AMGD1803
AMGD1804

site_idAC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE MGD A 1803
ChainResidue
AARG20
AGLN123
AASN148
ACYS152
AGLN350
AGLN384
AVAL454
AASN455
AASN456
AASN457
AALA460
ASER482
AASP483
AALA484
ATHR487
ASER499
AALA500
AMET501
ALYS505
AASP532
ATHR692
AARG694
ATRP699
AHIS700
ASER701
ASER703
ATRP768
AASN776
APHE792
ALYS793
AHOH820
AHOH826
AHOH860
AMOS1802
AMGD1804

site_idAC4
Number of Residues37
DetailsBINDING SITE FOR RESIDUE MGD A 1804
ChainResidue
ACYS22
ALYS56
ACYS152
ATRP185
AGLY186
AASN188
AGLU191
AMET192
ASER216
ATHR217
APHE218
AHIS220
APHE232
AGLN235
AASP237
ATHR345
AMET346
AGLY347
APHE348
AGLY383
AGLN384
AGLY693
AARG694
AVAL695
ALEU696
AHIS698
ATRP699
AHIS700
ALYS793
ALYS794
AHOH871
AHOH888
AHOH894
AHOH940
AHOH1030
AMOS1802
AMGD1803

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 803
ChainResidue
APHE397
AHIS399
AARG400
AHOH1090
AHOH1200

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 804
ChainResidue
ALEU241
AASN242
AALA245
AMET360
AASN363
ALEU364

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 805
ChainResidue
ATYR587
AFMT815
AHOH883
AHOH1216
ASER15
ALYS16
AHIS520

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 806
ChainResidue
AARG150
AHIS399
AILE786
AHOH1279
AHOH1297

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 807
ChainResidue
AASP167
AGLU168
AARG392
AGLU393
AASP404
AHIS616
ATRP632
AHOH817

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 809
ChainResidue
AARG734

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 810
ChainResidue
AALA627
AARG628
AHOH1361

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 811
ChainResidue
AGLY229
AILE230
AILE231
ALYS325
AHOH1126

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 812
ChainResidue
AARG203
AHOH1322

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 813
ChainResidue
AARG733
AARG734
AHOH1408

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 814
ChainResidue
AGLY527
AGLU528
AALA529
AARG530
AHOH960

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 815
ChainResidue
AGLU626
AFMT805

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 816
ChainResidue
ASER772
ALEU774
ALYS777
BARG7

site_idBC9
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC B 1128
ChainResidue
BPRO40
BTHR41
BILE42
BPRO43
BHIS44
BILE46
BTYR49
BARG57
BCYS58
BCYS61
BHIS62
BALA72
BILE73
BCYS98
BHIS102
BFMT140
BHOH355
BHOH667

site_idCC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC B 1129
ChainResidue
AASN53
ATYR58
BGLN38
BPRO39
BPRO40
BILE73
BVAL75
BSER76
BTHR78
BHIS79
BARG95
BPHE97
BCYS98
BCYS101
BHIS102
BHOH162
BHOH409
BHOH568
BHOH667

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 135
ChainResidue
BGLY48
BTYR49
BGLN50
BARG57

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 136
ChainResidue
ALYS109
AARG746
BALA13
BASN14
BGLU15
BHOH144

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B 137
ChainResidue
BGLY113
BASN114

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 138
ChainResidue
BLEU2
BVAL3
BHOH767

site_idCC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 139
ChainResidue
ALEU491
BVAL3
BASP4
BARG7
BGLY8
BHOH684
BHOH710

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 140
ChainResidue
BHIS44
BTYR49
BHEC1128

Functional Information from PROSITE/UniProt
site_idPS00551
Number of Residues19
DetailsMOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. ApCrf.CGTgCgVtVavkdN
ChainResidueDetails
AALA17-ASN35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1
ChainResidueDetails
BHIS44
ASER216
AGLN235
AMET346
AGLN350
AASN456
ASER482
ALYS505
AASP532
ATHR692
AASN776
BHIS62
ALYS793
BHIS79
BHIS102
ALYS56
AGLN123
AASN148
ACYS152
ATRP185

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1
ChainResidueDetails
BCYS58
BCYS61
BCYS98
BCYS101

218853

PDB entries from 2024-04-24

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