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1HBR

R-STATE FORM OF CHICKEN HEMOGLOBIN D

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0046872molecular_functionmetal ion binding
A0048821biological_processerythrocyte development
B0005344molecular_functionoxygen carrier activity
B0005615cellular_componentextracellular space
B0005623cellular_componentobsolete cell
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030492molecular_functionhemoglobin binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0046872molecular_functionmetal ion binding
B0048821biological_processerythrocyte development
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005833cellular_componenthemoglobin complex
C0015671biological_processoxygen transport
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0046872molecular_functionmetal ion binding
C0048821biological_processerythrocyte development
D0005344molecular_functionoxygen carrier activity
D0005615cellular_componentextracellular space
D0005623cellular_componentobsolete cell
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0030492molecular_functionhemoglobin binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0046872molecular_functionmetal ion binding
D0048821biological_processerythrocyte development
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
AVAL93
AASN97
APHE98
ALEU101
AHOH143
AHOH144
AHOH156
APHE43
AHIS45
APHE46
AHIS58
ALYS61
ALEU83
AHIS87
ALEU91

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BTHR38
BPHE41
BPHE42
BHIS63
BLYS66
BSER70
BLEU88
BHIS92
BVAL98
BASN102
BLEU106
BLEU141
BHOH148
BHOH149
BHOH165

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM C 142
ChainResidue
CTYR42
CPHE43
CHIS45
CPHE46
CHIS58
CLEU83
CHIS87
CLEU91
CVAL93
CASN97
CPHE98
CLEU101
CHOH145
CHOH172

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM D 147
ChainResidue
DPHE41
DPHE42
DHIS63
DLYS66
DLEU88
DHIS92
DLEU96
DVAL98
DASN102
DPHE103
DLEU106
DLEU141
DHOH148
DHOH149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues424
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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