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1HJ3

Cytochrome cd1 Nitrite Reductase, dioxygen complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050418molecular_functionhydroxylamine reductase activity
A0050421molecular_functionnitrite reductase (NO-forming) activity
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0050418molecular_functionhydroxylamine reductase activity
B0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 621
ChainResidue
ATYR308
AARG354
ALYS372

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 621
ChainResidue
BTYR308
BARG354
BLYS372
BHOH2279
BHOH2407

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 622
ChainResidue
BGLY440
BASN461
BHOH2305
BHOH2315
BGLY439

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEC A 601
ChainResidue
AHIS17
AARG64
ACYS65
ACYS68
AHIS69
AGLY78
ALYS79
ALEU81
ALEU89
ATYR93
ALEU94
APHE97
ASER102
APRO103

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR RESIDUE DHE A 602
ChainResidue
ATYR25
APRO27
ASER28
AMET106
AARG174
AHIS200
AILE201
AARG203
AARG216
AARG243
ASER244
AILE245
ATYR263
AALA302
AILE303
AHIS345
AARG391
APHE444
AGLN507
ATRP522
ATHR554
AGLY555
APHE557
AHOH2002
AHOH2189
AHOH2385
AHOH2386
AHOH2387

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC B 601
ChainResidue
BARG64
BCYS65
BCYS68
BHIS69
BTHR77
BGLY78
BLYS79
BTYR93
BLEU94
BPHE97
BILE98
BALA104
BGLY105
BMET106
BTRP109
BHOH2402

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE DHE B 602
ChainResidue
BPRO27
BSER28
BARG174
BHIS200
BILE201
BARG203
BARG216
BARG243
BSER244
BILE245
BTYR263
BALA302
BILE303
BHIS345
BARG391
BPHE444
BGLN507
BTRP522
BGLY555
BPHE557
BOXY603
BHOH2189
BHOH2403
BHOH2404
BHOH2405
BHOH2406

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY B 603
ChainResidue
BDHE602
BHIS345
BHIS388

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 611
ChainResidue
APHE395
AVAL396
APRO449
ASER451
AILE475
AHOH2298
AHOH2388

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 612
ChainResidue
BASP30
BARG174
BTYR197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:7736589, ECO:0007744|PDB:1QKS
ChainResidueDetails
AHIS17
ATYR25
AHIS69
AHIS200
BHIS17
BTYR25
BHIS69
BHIS200

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:7736589, ECO:0007744|PDB:1QKS
ChainResidueDetails
ASER28
AARG391
AGLN507
ATHR554
BSER28
BLYS79
BTYR93
BTRP109
BARG174
BARG203
BARG216
ALYS79
BARG243
BTYR263
BARG391
BGLN507
BTHR554
ATYR93
ATRP109
AARG174
AARG203
AARG216
AARG243
ATYR263

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:7736589, ECO:0007744|PDB:1QKS
ChainResidueDetails
ACYS65
ACYS68
BCYS65
BCYS68

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nir
ChainResidueDetails
AHIS388
AHIS345

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nir
ChainResidueDetails
BHIS388
BHIS345

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PDB entries from 2024-11-13

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