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1YVT

The high salt (phosphate) crystal structure of CO Hemoglobin E (Glu26Lys) at physiological pH (pH 7.35)

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
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
A0043177molecular_functionorganic acid binding
A0046872molecular_functionmetal ion binding
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
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
B0043177molecular_functionorganic acid binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0046872molecular_functionmetal ion binding
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 Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
ATYR42
ALEU91
AVAL93
AASN97
APHE98
ALEU101
ALEU136
ACMO501
AHOH545
AHOH553
APHE43
AHIS45
AHIS58
ALYS61
AALA65
ALEU83
ALEU86
AHIS87

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 402
ChainResidue
APRO4
BTHR38
BPHE41
BPHE42
BHIS63
BLYS66
BLEU88
BHIS92
BLEU96
BVAL98
BASN102
BLEU106
BLEU141
BCMO502
BHOH528
BHOH543
BHOH549
BHOH669

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 501
ChainResidue
AHIS58
AVAL62
AHEM401

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 502
ChainResidue
BHIS63
BVAL67
BHEM402

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
AVAL96
ALYS99
ALYS99
BGLU101
BGLU101
BHOH510
BHOH515
BHOH544
BHOH567

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BHIS2
BLEU3
BGLY83
BLYS144

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: distal binding residue
ChainResidueDetails
BGLY64

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
BCYS93
AARG92
AVAL107
ALEU109
AHIS122
ATHR134
ATRP14
AGLY25
AGLU30
APHE46
ALEU48
AALA53
ALYS56
ALYS60

site_idSWS_FT_FI4
Number of Residues19
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
BLYS8
BLEU75
BPHE85
BCYS93
BLEU105
BVAL111
BLYS120
BTHR123
BALA129
BLEU141
BTYR145
BLYS26
BARG30
BPRO36
BTHR38
BGLY46
BALA53
BASN57
BSER72

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
BVAL60
BGLY83
BLEU96

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-pyruvate 2-iminyl-valine; in Hb A1b
ChainResidueDetails
BHIS2
AVAL17
ATHR41

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BALA10
BPHE45

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BALA13
BPRO51
BLEU88

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:4531009
ChainResidueDetails
BVAL60
BGLY83

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
ChainResidueDetails
BASP94
ALEU125
AVAL132
ALYS139

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
ChainResidueDetails
BTYR145
AVAL135
ASER138

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
ChainResidueDetails
BHIS2
AVAL17
ATHR41

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
BSER9
BVAL18
BVAL67
BGLU121

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
BTYR145

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PDB entries from 2024-12-18

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