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3PT7

Structure of HbII-III-Oxy from Lucina pectinata at pH 5.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
B0001666biological_processresponse to hypoxia
B0005344molecular_functionoxygen carrier activity
B0005737cellular_componentcytoplasm
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
ATHR40
AHIS97
AARG100
AILE102
ALEU107
ATYR111
AHOH168
AHOH169
AHOH178
AHOH187
AOXY501
APRO43
BLYS93
BLEU97
BHOH191
BHOH200
APHE44
ALEU47
AGLN65
AVAL68
AMET73
AMET93
ALEU96

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY A 501
ChainResidue
ATYR30
AGLN65
AHEM500

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
ALYS92
BTHR41
BPRO44
BPHE45
BLEU48
BGLN66
BVAL69
BPHE70
BMET74
BMET94
BLEU97
BHIS98
BARG101
BILE103
BGLU107
BLEU108
BTYR112
BHOH162
BHOH166
BHOH168
BHOH172
BHOH180
BHOH190
BOXY501

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY B 501
ChainResidue
BTYR31
BPHE45
BGLN66
BHEM500

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 153
ChainResidue
BGLN92
BHOH160
BHOH200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
BHIS98

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:8397786
ChainResidueDetails
BSER1

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PDB entries from 2024-09-04

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