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4O6Y

Crystal Structure of Cytochrome b561

Functional Information from GO Data
ChainGOidnamespacecontents
A0000293molecular_functionferric-chelate reductase activity
A0005794cellular_componentGolgi apparatus
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0019852biological_processL-ascorbic acid metabolic process
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0140571molecular_functiontransmembrane ascorbate ferrireductase activity
B0000293molecular_functionferric-chelate reductase activity
B0005794cellular_componentGolgi apparatus
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019852biological_processL-ascorbic acid metabolic process
B0046872molecular_functionmetal ion binding
B0055085biological_processtransmembrane transport
B0140571molecular_functiontransmembrane ascorbate ferrireductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 301
ChainResidue
ATRP29
AHIS118
ASER119
AGLY122
ATHR171
AALA172
AGLY175
AILE176
AGLU178
ALYS179
AHOH416
APHE48
AHIS51
AMET55
ALEU103
AHIS106
AASN113
APHE114
ASER116

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 302
ChainResidue
AMET67
ATYR70
ALYS71
AHIS84
AGLN88
APHE129
AGLN132
ATRP133
AGLY136
APHE137
ATYR140
ATRP141
AARG147
AMET154
AHIS157
AVAL158
AGLY161
AVAL217
AHOH409

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ALYS81
ATYR140
AARG147
AARG150
AARG150

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 301
ChainResidue
BTRP29
BPHE48
BHIS51
BMET55
BLEU59
BLEU103
BHIS106
BASN113
BPHE114
BSER116
BHIS118
BSER119
BGLY122
BTHR171
BALA172
BGLY175
BILE176
BGLU178
BLYS179
BHOH403

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 302
ChainResidue
BMET67
BTYR70
BLYS71
BLYS81
BHIS84
BGLN88
BPHE129
BGLN132
BTRP133
BGLY136
BPHE137
BTYR140
BTRP141
BMET154
BHIS157
BVAL158
BHOH401
BHOH409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues408
DetailsDomain: {"description":"Cytochrome b561","evidences":[{"source":"PROSITE-ProRule","id":"PRU00242","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"24449903","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24449903","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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