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1ASH

THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 301
ChainResidue
ALEU40
ATRP108
APHE111
APHE140
AOXY302
ATYR43
APHE44
AGLN64
ALYS67
AALA71
AARG95
AHIS96
AMET103

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 302
ChainResidue
ATYR30
APHE44
AGLN64
AHEM301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1584800","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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