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1I3D

HUMAN CARBONMONOXY HEMOGLOBIN BART'S (GAMMA4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005829cellular_componentcytosol
A0005833cellular_componenthemoglobin complex
A0015670biological_processcarbon dioxide transport
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031720molecular_functionhaptoglobin binding
A0031721molecular_functionhemoglobin alpha binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0042744biological_processhydrogen peroxide catabolic process
A0043177molecular_functionorganic acid binding
A0046872molecular_functionmetal ion binding
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005829cellular_componentcytosol
B0005833cellular_componenthemoglobin complex
B0015670biological_processcarbon dioxide transport
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 147
ChainResidue
APHE41
AASN102
APHE103
ALEU106
ALEU141
ACMO148
AHOH347
AHOH441
AHOH472
BSER50
APHE42
AHIS63
ALYS66
ASER70
ALEU88
AHIS92
ALEU96
AVAL98

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 148
ChainResidue
AHIS63
AVAL67
AHEM147

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
ASER50
ASER52
AHOH332
BPHE41
BPHE42
BPHE45
BHIS63
BVAL67
BSER70
BLEU91
BHIS92
BLEU96
BVAL98
BASN102
BLEU106
BLEU141
BCMO148
BHOH390

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BHIS63
BVAL67
BHEM147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000250|UniProtKB:P80044
ChainResidueDetails
AGLY64
BGLY64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:11514664, ECO:0007744|PDB:1I3D, ECO:0007744|PDB:1I3E
ChainResidueDetails
ACYS93
BCYS93

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylglycine; in form Hb F1 => ECO:0000269|PubMed:5554303
ChainResidueDetails
AHIS2
BHIS2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
ASER13
BSER13

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE45
AALA51
AALA53
AALA140
BPHE45
BALA51
BALA53
BALA140

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
AVAL60
AGLY83
BVAL60
BGLY83

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
AASP94
BASP94

218500

PDB entries from 2024-04-17

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