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3PI3

Crystallographic Structure of HbII-oxy from Lucina pectinata at pH 5.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
APRO43
AILE102
ALEU107
AALA110
ATYR111
AHOH209
AHOH210
AHOH234
AHOH258
AHOH261
AHOH279
APHE44
AOXY501
BLYS92
BLEU96
ALEU47
AGLN65
AVAL68
AMET73
ALEU96
AHIS97
AARG100

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 501
ChainResidue
ATYR30
APHE44
AGLN65
AHEM500

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
ALYS92
BTHR40
BPRO43
BPHE44
BLEU47
BGLN65
BVAL68
BPHE69
BMET73
BMET93
BLEU96
BHIS97
BARG100
BILE102
BLEU107
BALA110
BTYR111
BHOH157
BHOH186
BHOH197
BHOH203
BHOH221
BHOH247
BOXY501

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY B 501
ChainResidue
BTYR30
BPHE44
BGLN65
BHEM500

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS97
BHIS97

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0000269|PubMed:1815587
ChainResidueDetails
ATHR1
BTHR1

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PDB entries from 2024-07-31

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