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1FDH

STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN

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
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005829cellular_componentcytosol
B0005833cellular_componenthemoglobin complex
B0015670biological_processcarbon dioxide transport
B0015671biological_processoxygen transport
B0016020cellular_componentmembrane
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030185biological_processnitric oxide transport
B0031720molecular_functionhaptoglobin binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071682cellular_componentendocytic vesicle lumen
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
G0004601molecular_functionperoxidase activity
G0005344molecular_functionoxygen carrier activity
G0005515molecular_functionprotein binding
G0005829cellular_componentcytosol
G0005833cellular_componenthemoglobin complex
G0015670biological_processcarbon dioxide transport
G0015671biological_processoxygen transport
G0019825molecular_functionoxygen binding
G0020037molecular_functionheme binding
G0031720molecular_functionhaptoglobin binding
G0031721molecular_functionhemoglobin alpha binding
G0031838cellular_componenthaptoglobin-hemoglobin complex
G0042744biological_processhydrogen peroxide catabolic process
G0043177molecular_functionorganic acid binding
G0046872molecular_functionmetal ion binding
G0072562cellular_componentblood microparticle
G0098869biological_processcellular oxidant detoxification
H0004601molecular_functionperoxidase activity
H0005344molecular_functionoxygen carrier activity
H0005515molecular_functionprotein binding
H0005829cellular_componentcytosol
H0005833cellular_componenthemoglobin complex
H0015670biological_processcarbon dioxide transport
H0015671biological_processoxygen transport
H0019825molecular_functionoxygen binding
H0020037molecular_functionheme binding
H0031720molecular_functionhaptoglobin binding
H0031721molecular_functionhemoglobin alpha binding
H0031838cellular_componenthaptoglobin-hemoglobin complex
H0042744biological_processhydrogen peroxide catabolic process
H0043177molecular_functionorganic acid binding
H0046872molecular_functionmetal ion binding
H0072562cellular_componentblood microparticle
H0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
ALEU91
AVAL93
AASN97
APHE98
ALEU101
ALEU136
APHE43
AHIS45
APHE46
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM G 147
ChainResidue
GHIS63
GVAL67
GSER70
GPHE85
GLEU88
GLEU91
GHIS92
GLEU96
GASN102
GLEU106
GLEU141
HGLU5

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 142
ChainResidue
BTYR42
BPHE43
BHIS45
BPHE46
BHIS58
BLYS61
BLEU83
BLEU86
BHIS87
BLEU91
BVAL93
BASN97
BPHE98
BLEU101
BLEU136

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM H 147
ChainResidue
BHIS72
HHIS63
HVAL67
HSER70
HPHE85
HLEU88
HLEU91
HHIS92
HLEU96
HASN102
HLEU106
HLEU141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: distal binding residue => ECO:0000250|UniProtKB:P80044
ChainResidueDetails
GPRO58
HPRO58
GHIS63
HHIS63

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:11514664, ECO:0007744|PDB:1I3D, ECO:0007744|PDB:1I3E
ChainResidueDetails
GGLN87
HGLN87

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
GASP7
AARG92
AVAL107
ALEU109
AHIS122
ATHR134
BASN9
BTRP14
BGLY25
BGLU30
BPHE46
HASP7
BLEU48
BALA53
BLYS56
BLYS60
BARG92
BVAL107
BLEU109
BHIS122
BTHR134
GTHR12
HTHR12
APHE46
ALEU48
AALA53
ALYS56
ALYS60

site_idSWS_FT_FI4
Number of Residues20
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
GGLN39
GSER50
GSER52
GSER139
GSER142
GSER143
HSER44
HSER50
HSER52
HSER139
HSER142
GPHE45
HSER143
GASN47
GVAL134
HGLN39
HPHE45
HASN47
HVAL134
GSER44

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
GILE54
GHIS77
HILE54
HHIS77
GLYS59
GLYS82
HLYS59
HLYS82

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
GLEU88
HLEU88
GCYS93
HCYS93
BVAL17
BTHR41

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:881729, ECO:0007744|PDB:1FDH, ECO:0007744|PDB:4MQJ, ECO:0007744|PDB:4MQK
ChainResidueDetails
GHIS92
HHIS92

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N-acetylglycine; in form Hb F1 => ECO:0000269|PubMed:5554303
ChainResidueDetails
GGLY1
HGLY1

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY25
BGLY25

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
AHIS103
ALEU125
AVAL132
ALYS139
BHIS103
BLEU125
BVAL132
BLYS139

site_idSWS_FT_FI11
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALEU109
AVAL135
ASER138
BLEU109
BVAL135
BSER138

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
ATHR8
AVAL17
ATHR41
BTHR8
BVAL17
BTHR41

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
AVAL62
BVAL62

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PDB entries from 2024-11-06

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