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1SPG

CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031720molecular_functionhaptoglobin binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0042744biological_processhydrogen peroxide catabolic process
A0043177molecular_functionorganic acid binding
A0046872molecular_functionmetal ion binding
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005829cellular_componentcytosol
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 144
ChainResidue
ATYR42
AVAL95
AASN99
APHE100
ALEU103
ALEU134
ACMO145
AHOH311
BTHR4
BASP5
APHE43
ATRP46
AHIS60
AVAL63
AILE64
AALA67
AVAL68
AHIS89

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 145
ChainResidue
AHIS60
AILE64
AHEM144

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 148
ChainResidue
BHIS41
BHIS63
BTHR66
BHIS92
BILE96
BVAL98
BASN102
BLEU142
BCMO149
BHOH353

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 149
ChainResidue
BHIS63
BVAL67
BHEM148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"8605630","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues145
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"distal binding residue","evidences":[{"source":"UniProtKB","id":"P80044","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"8605630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SPG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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