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1HBG

GLYCERA DIBRANCHIATA HEMOGLOBIN. STRUCTURE AND REFINEMENT AT 1.5 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 148
ChainResidue
APHE45
ACMO201
AHOH279
AHOH343
ALEU58
AARG89
AHIS90
ATYR93
AGLY94
ATYR102
APHE103
ALEU141

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CMO A 201
ChainResidue
APHE45
ALEU58
AVAL62
AHEM148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS90

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Causes a bend in the G helix
ChainResidueDetails
APRO105

218853

PDB entries from 2024-04-24

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