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2OLP

Structure and ligand selection of hemoglobin II from Lucina pectinata

Functional Information from GO Data
ChainGOidnamespacecontents
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 200
ChainResidue
AHIS37
AHOH549
BTHR1
BLYS8
BASN83
BHOH533
BHOH538
BHOH593

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 200
ChainResidue
ASER16
AHOH519
AHOH523
AHOH586
AARG12

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
APRO43
APHE44
ALEU47
AGLN65
AMET93
ALEU96
AHIS97
AARG100
AILE102
ALEU107
AALA110
ATYR111
AHOH504
AHOH505
AHOH506
AHOH520
AHOH526
AHOH535
BLYS92

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY A 501
ChainResidue
ATYR30
APHE44
AGLN65

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
ALYS92
BPRO43
BPHE44
BLEU47
BGLN65
BPHE69
BLEU96
BHIS97
BARG100
BILE102
BLEU107
BTYR111
BHOH502
BHOH503
BHOH504
BHOH505
BHOH516
BHOH565

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OXY B 501
ChainResidue
BTYR30
BGLN65

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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