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1AOF

CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED FORM

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 Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 601
ChainResidue
AGLY78
ALYS79
ALEU81
ATYR93
APHE97
ASER102
AALA104
AGLY105
AMET106
ATRP109
AARG64
ACYS65
ACYS68
AHIS69
ATHR77

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE DHE A 602
ChainResidue
AARG174
AHIS200
AILE201
AARG203
AARG216
AARG243
ASER244
ATYR263
AALA302
AILE303
AHIS345
AARG391
APHE444
AGLN507
ATHR554
APHE557
ASO2603
AHOH613
AHOH622
AHOH641
AHOH644
AHOH734

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO2 A 603
ChainResidue
AHIS345
AHIS388
APHE444
ADHE602

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 601
ChainResidue
BARG64
BCYS65
BCYS68
BHIS69
BGLY78
BLYS79
BTYR93
BSER102
BALA104
BMET106
BPRO107
BTRP109
BHOH880

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR RESIDUE DHE B 602
ChainResidue
BPRO27
BSER28
BARG174
BHIS200
BILE201
BARG203
BARG216
BARG243
BSER244
BTYR263
BALA302
BILE303
BHIS345
BARG391
BPHE444
BGLN507
BTHR554
BGLY555
BPHE557
BSO2603
BHOH604
BHOH623
BHOH633
BHOH636
BHOH637
BHOH715
BHOH746
BHOH850

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO2 B 603
ChainResidue
BHIS345
BHIS388
BPHE444
BDHE602

site_idC1A
Number of Residues1
DetailsTHE C HEM IS THE POINT OF ELECTRON ENTRY.
ChainResidue
AHEM601

site_idC1B
Number of Residues1
DetailsTHE C HEM IS THE POINT OF ELECTRON ENTRY.
ChainResidue
BHEM601

site_idD1A
Number of Residues1
DetailsTHE D HEM IS THE SITE OF CATALYTIC ACTIVITY.
ChainResidue
ADHE602

site_idD1B
Number of Residues1
DetailsTHE D HEM IS THE SITE OF CATALYTIC ACTIVITY.
ChainResidue
BDHE602

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 2024-07-10

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