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1YZI

A novel quaternary structure of human carbonmonoxy hemoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005829cellular_componentcytosol
A0005833cellular_componenthemoglobin complex
A0006954biological_processinflammatory response
A0015670biological_processcarbon dioxide transport
A0015671biological_processoxygen transport
A0016020cellular_componentmembrane
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0030185biological_processnitric oxide transport
A0031720molecular_functionhaptoglobin binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0048821biological_processerythrocyte development
A0070062cellular_componentextracellular exosome
A0071682cellular_componentendocytic vesicle lumen
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005829cellular_componentcytosol
B0005833cellular_componenthemoglobin complex
B0006954biological_processinflammatory response
B0008217biological_processregulation of blood pressure
B0015670biological_processcarbon dioxide transport
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030185biological_processnitric oxide transport
B0030492molecular_functionhemoglobin binding
B0031720molecular_functionhaptoglobin binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0046872molecular_functionmetal ion binding
B0048821biological_processerythrocyte development
B0070062cellular_componentextracellular exosome
B0070293biological_processrenal absorption
B0070527biological_processplatelet aggregation
B0071682cellular_componentendocytic vesicle lumen
B0072562cellular_componentblood microparticle
B0097746biological_processblood vessel diameter maintenance
B0098869biological_processcellular oxidant detoxification
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 142
ChainResidue
AHIS58
AVAL62
AHEM143

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CMO B 147
ChainResidue
BVAL67
BHEM148

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 143
ChainResidue
AHIS58
ALYS61
AALA65
ALEU83
AHIS87
ALEU91
AVAL93
AASN97
APHE98
ALEU101
ALEU136
ACMO142
AHOH281
ATHR39
ATYR42
APHE43
APHE46

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 148
ChainResidue
BTHR38
BPHE41
BPHE42
BHIS63
BLYS66
BVAL67
BPHE71
BLEU88
BLEU91
BHIS92
BLYS95
BLEU96
BASN102
BLEU106
BLEU141
BCMO147
BHOH176

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MBN A 201
ChainResidue
ATRP14
AALA63
ATHR67
AMBN205

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MBN A 203
ChainResidue
AALA12
AALA13
ALYS16
AGLU116
BASP52
BGLY56

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MBN A 205
ChainResidue
ATYR24
ALEU105
ALEU109
AMBN201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsPeptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues284
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues33
DetailsSite: {"description":"(Microbial infection) Cleavage; by N.americanus apr-2","evidences":[{"source":"PubMed","id":"12552433","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues9
DetailsPeptide: {"description":"LVV-hemorphin-7","featureId":"PRO_0000296641"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues6
DetailsPeptide: {"description":"Spinorphin","featureId":"PRO_0000424226"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N-pyruvate 2-iminyl-valine; in Hb A1b"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"8637569","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) valine; in Hb A1c","evidences":[{"source":"PubMed","id":"635569","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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