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5UCA

Crystal structure of human Heme Oxygenase-2 in complex with Laurate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004392molecular_functionheme oxygenase (decyclizing) activity
A0006788biological_processheme oxidation
B0004392molecular_functionheme oxygenase (decyclizing) activity
B0006788biological_processheme oxidation
C0004392molecular_functionheme oxygenase (decyclizing) activity
C0006788biological_processheme oxidation
D0004392molecular_functionheme oxygenase (decyclizing) activity
D0006788biological_processheme oxidation
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue DAO B 301
ChainResidue
BGLU49
BLEU74
BARG156
BTYR187
BPHE234

site_idAC2
Number of Residues4
Detailsbinding site for residue DAO C 301
ChainResidue
CGLU49
CVAL54
CLEU74
CARG156

site_idAC3
Number of Residues8
Detailsbinding site for residue DAO D 301
ChainResidue
DVAL54
DALA70
DTHR77
DARG156
DTYR187
DASN230
DPHE234
DHOH404

Functional Information from PROSITE/UniProt
site_idPS00593
Number of Residues11
DetailsHEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYMG
ChainResidueDetails
ALEU149-GLY159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP
ChainResidueDetails
ALEU74
BLEU74
CLEU74
DLEU74

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP
ChainResidueDetails
AGLY183
DGLY183
DGLU228
DGLN232
AGLU228
AGLN232
BGLY183
BGLU228
BGLN232
CGLY183
CGLU228
CGLN232

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P09601
ChainResidueDetails
APHE189
BPHE189
CPHE189
DPHE189

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AALA31
BALA31
CALA31
DALA31

222415

PDB entries from 2024-07-10

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