Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6L5W

Carbonmonoxy human hemoglobin C in the R quaternary structure at 140 K: Light (2 min)

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 Residues15
Detailsbinding site for residue HEM A 201
ChainResidue
ATYR42
AVAL93
AASN97
APHE98
ALEU101
ALEU136
ACMO202
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues3
Detailsbinding site for residue CMO A 202
ChainResidue
AHIS58
AVAL62
AHEM201

site_idAC3
Number of Residues13
Detailsbinding site for residue HEM B 201
ChainResidue
APRO4
BPHE41
BPHE42
BHIS63
BLYS66
BPHE71
BLEU88
BHIS92
BLEU96
BASN102
BLEU141
BCMO202
BHOH303

site_idAC4
Number of Residues3
Detailsbinding site for residue CMO B 202
ChainResidue
BHIS63
BVAL67
BHEM201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
BHIS2
BLYS82
BHIS143
AHIS58

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS87

site_idSWS_FT_FI3
Number of Residues14
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
ATHR8
AALA13
ATYR24
ALEU29
AHIS45
AASP47
ASER52
AVAL55
AGLY59
ALEU91
ALEU106
ATHR108
AVAL121
ASER133

site_idSWS_FT_FI4
Number of Residues5
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
BPHE45
BASP52
BGLY56
BPHE71
BGLY74
BTHR84
BHIS92
BARG104
BLEU110
BGLY119
BPHE122
BALA128
BALA140
BLYS144
ALYS11
ALYS56
ALYS60
ALYS90
ALYS99

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER3
ASER35
ASER49

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALYS7
ALYS16
ALYS40

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER44
ATHR8

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BTHR87
ALYS11
BTHR50

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR24
BLYS82

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ASER138
ASER102
ASER124
ASER131

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR134
ATHR137
ATHR108

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
ALYS16
ALYS40
ALYS7

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
BLYS17
BLYS66
BLYS120
ALYS61

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
BLYS144

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon