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2GDM

LEGHEMOGLOBIN (OXY)

Replaces:  1GDM
Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0010167biological_processresponse to nitrate
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 154
ChainResidue
ALEU43
ALYS100
AVAL102
AHIS106
APHE107
AVAL110
ATYR138
AOXY155
AHOH293
AHOH411
APHE44
ASER45
AHIS63
ALYS66
AVAL67
ALEU70
ALEU93
AHIS97

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 155
ChainResidue
AHIS63
AVAL67
AHEM154
AHOH412

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPeLqaHAgkvF
ChainResidueDetails
AASN57-PHE68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AALA64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AVAL98

218853

PDB entries from 2024-04-24

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