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3ML1

Crystal Structure of the Periplasmic Nitrate Reductase from Cupriavidus necator

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0008940molecular_functionnitrate reductase activity
A0009055molecular_functionelectron transfer activity
A0009325cellular_componentnitrate reductase complex
A0016020cellular_componentmembrane
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 Residues11
DetailsBINDING SITE FOR RESIDUE SF4 A 1801
ChainResidue
ACYS19
APRO194
AILE195
APHE21
ACYS22
AGLY25
ACYS26
AASN53
ACYS54
ALYS56
AGLY57

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MOS A 1802
ChainResidue
ACYS152
AGLN384
AARG694
AMGD1803
AMGD1804

site_idAC3
Number of Residues34
DetailsBINDING SITE FOR RESIDUE MGD A 1803
ChainResidue
AARG20
AGLN123
AASN148
ACYS152
AGLN350
AGLN384
AVAL454
AASN455
AASN456
AASN457
AALA460
ASER482
AASP483
ATHR487
ASER499
AALA500
AMET501
ALYS505
AASP532
ATHR692
AARG694
ATRP699
AHIS700
ASER701
ASER703
ATRP768
AASN776
APHE792
ALYS793
AHOH860
AHOH937
AHOH991
AMOS1802
AMGD1804

site_idAC4
Number of Residues38
DetailsBINDING SITE FOR RESIDUE MGD A 1804
ChainResidue
ACYS22
ALYS56
ACYS152
ATRP185
AGLY186
AASN188
AGLU191
AMET192
ASER216
ATHR217
APHE218
AHIS220
APHE232
APRO234
AGLN235
AASP237
ATHR345
AMET346
AGLY347
APHE348
AGLY383
AGLN384
AGLY693
AARG694
AVAL695
ALEU696
AHIS698
ATRP699
AHIS700
ALYS793
ALYS794
AHOH803
AHOH871
AHOH943
AHOH956
AHOH985
AMOS1802
AMGD1803

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEC B 1128
ChainResidue
BHIS102
BHOH455
BHEC1129
BPRO40
BPRO43
BHIS44
BTYR49
BARG57
BCYS58
BCYS61
BHIS62
BALA72
BILE73
BCYS98

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEC B 1129
ChainResidue
AASN53
ATYR58
BGLN38
BILE73
BVAL75
BSER76
BILE77
BTHR78
BHIS79
BARG95
BPHE97
BCYS98
BCYS101
BHIS102
BHOH141
BHOH215
BHOH302
BHOH353
BHOH455
BHOH513
BHOH553
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

237735

PDB entries from 2025-06-18

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