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1T1N

CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031720molecular_functionhaptoglobin 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
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin 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 Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 143
ChainResidue
ALYS62
AGLN87
AHIS88
ALEU92
AASN98
ALEU102
ALEU137
ACMO144
ATYR42
APHE43
AHIS45
ATRP46
AHIS59

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 144
ChainResidue
AHIS59
AVAL63
AHEM143

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BTYR41
BPHE42
BHIS63
BLYS66
BHIS92
BLEU96
BVAL98
BASN102
BPHE103
BLEU106
BLEU141
BCMO148

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

site_idSTA
Number of Residues2
DetailsHEME GROUPS ARE BOUND TO CO
ChainResidue
AHIS88
AHEM143

site_idSTB
Number of Residues2
DetailsHEME GROUPS ARE BOUND TO CO
ChainResidue
BHIS92
BHEM147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"8144556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues144
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"distal binding residue","evidences":[{"source":"PubMed","id":"12093902","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LA6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"12093902","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NG6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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