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1KFR

Structural plasticity in the eight-helix fold of a trematode hemoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ATHR3
AHIS5
ASER47
AARG48
AHOH1041
AHOH1080
AHOH1140
AHOH1173

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ASER60
AASP61
AASP125
AALA126
AGLU127
AHOH1007
AHOH1037
AHOH1159
AHIS52

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AHIS65
AARG68
AHOH1043

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 148
ChainResidue
ATYR32
AHIS45
APHE46
ATYR66
ATHR69
ALEU70
AHIS98
AGLU107
APHE108
APHE115
APHE140
AMET143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues146
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

247536

PDB entries from 2026-01-14

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