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1IRD

Crystal Structure of Human Carbonmonoxy-Haemoglobin at 1.25 A Resolution

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 Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
AVAL93
AASN97
APHE98
ALEU101
ALEU136
ACMO143
AHOH2134
AHOH2138
AHOH2214
AHOH2215
APHE43
AHOH2259
AHIS45
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CMO A 143
ChainResidue
ALEU29
AHIS58
AVAL62
AHEM142

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 347
ChainResidue
APRO4
AHOH2163
AHOH2235
BTHR238
BPHE241
BPHE242
BHIS263
BLYS266
BPHE271
BLEU288
BHIS292
BLEU296
BASN302
BLEU341
BCMO348
BHOH2035
BHOH2036
BHOH2082
BHOH2111

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 348
ChainResidue
BHIS263
BVAL267
BHEM347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AGLY59
BLEU203
BGLY283
BLYS344

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AALA88

site_idSWS_FT_FI3
Number of Residues14
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
AASN9
AARG92
AVAL107
ALEU109
AHIS122
ATHR134
ATRP14
AGLY25
AGLU30
APHE46
ALEU48
AALA53
ALYS56
ALYS60

site_idSWS_FT_FI4
Number of Residues5
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
AALA12
BLEU275
BPHE285
BCYS293
BLEU305
BVAL311
BLYS320
BTHR323
BALA329
BLEU341
BTYR345
AGLY57
ALYS61
ALEU91
ALEU100
BGLY246
BALA253
BASN257
BSER272

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
APRO4
APHE36
AHIS50

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR8
AVAL17
ATHR41

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AASN9
BPHE245

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
AALA12
BPRO251
BLEU288

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY25
BGLY283

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
AHIS103
ALEU125
AVAL132
ALYS139

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALEU109
AVAL135
ASER138

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
ATHR8
AVAL17
ATHR41

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
AVAL62
BVAL218
BVAL267
BGLU321

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
BTYR345

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PDB entries from 2024-08-14

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