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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1SDK

CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A

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
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005829cellular_componentcytosol
C0005833cellular_componenthemoglobin complex
C0006954biological_processinflammatory response
C0015670biological_processcarbon dioxide transport
C0015671biological_processoxygen transport
C0016020cellular_componentmembrane
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0030185biological_processnitric oxide transport
C0031720molecular_functionhaptoglobin binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0042542biological_processresponse to hydrogen peroxide
C0042744biological_processhydrogen peroxide catabolic process
C0046872molecular_functionmetal ion binding
C0048821biological_processerythrocyte development
C0070062cellular_componentextracellular exosome
C0071682cellular_componentendocytic vesicle lumen
C0072562cellular_componentblood microparticle
C0098869biological_processcellular oxidant detoxification
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005829cellular_componentcytosol
D0005833cellular_componenthemoglobin complex
D0006954biological_processinflammatory response
D0008217biological_processregulation of blood pressure
D0015670biological_processcarbon dioxide transport
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0030185biological_processnitric oxide transport
D0030492molecular_functionhemoglobin binding
D0031720molecular_functionhaptoglobin binding
D0031721molecular_functionhemoglobin alpha binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042542biological_processresponse to hydrogen peroxide
D0042744biological_processhydrogen peroxide catabolic process
D0045429biological_processpositive regulation of nitric oxide biosynthetic process
D0046872molecular_functionmetal ion binding
D0048821biological_processerythrocyte development
D0070062cellular_componentextracellular exosome
D0070293biological_processrenal absorption
D0070527biological_processplatelet aggregation
D0071682cellular_componentendocytic vesicle lumen
D0072562cellular_componentblood microparticle
D0097746biological_processblood vessel diameter maintenance
D0098869biological_processcellular oxidant detoxification
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ATYR42
AASN97
APHE98
ALEU136
ACMO201
DASP47
DTHR50
DHOH360
DHOH390
DHOH391
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
AHIS87
ALEU91
AVAL93
site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 201
ChainResidue
AHIS58
AVAL62
AHEM200
site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BTHR38
BPHE41
BPHE42
BHIS63
BLYS66
BPHE71
BHIS92
BLEU96
BASN102
BLEU106
BLEU141
BCMO201
BHOH248
BHOH259
BHOH300
site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 201
ChainResidue
BHIS63
BVAL67
BHEM200
site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM C 200
ChainResidue
CTYR42
CPHE43
CHIS58
CLYS61
CLEU86
CHIS87
CLEU91
CVAL93
CASN97
CPHE98
CLEU101
CLEU136
CCMO201
site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CMO C 201
ChainResidue
CPHE43
CHIS58
CVAL62
CHEM200
site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM D 200
ChainResidue
DPHE41
DPHE42
DHIS63
DLYS66
DHIS92
DVAL98
DASN102
DPHE103
DLEU141
DCMO201
DHOH328
site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO D 201
ChainResidue
DHIS63
DVAL67
DHEM200
site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TMM D 300
ChainResidue
BLYS82
BHIS143
BHIS146
CHOH287
DVAL1
DHIS2
DLYS82
DHOH373
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsPeptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues568
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues66
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 Residues16
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues18
DetailsPeptide: {"description":"LVV-hemorphin-7","featureId":"PRO_0000296641"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues12
DetailsPeptide: {"description":"Spinorphin","featureId":"PRO_0000424226"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"N-pyruvate 2-iminyl-valine; in Hb A1b"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
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 Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) valine; in Hb A1c","evidences":[{"source":"PubMed","id":"635569","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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건을2025-07-23부터공개중

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