5UC8

Crystal structure of human Heme Oxygenase-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004392	molecular_function	heme oxygenase (decyclizing) activity
A	0006788	biological_process	heme oxidation
B	0004392	molecular_function	heme oxygenase (decyclizing) activity
B	0006788	biological_process	heme oxidation
C	0004392	molecular_function	heme oxygenase (decyclizing) activity
C	0006788	biological_process	heme oxidation
D	0004392	molecular_function	heme oxygenase (decyclizing) activity
D	0006788	biological_process	heme oxidation

Functional Information from PROSITE/UniProt

site_id	PS00593
Number of Residues	11
Details	HEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYMG

Chain	Residue	Details
A	LEU149-GLY159

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP

Chain	Residue	Details
A	LEU74
B	LEU74
C	LEU74
D	LEU74

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:17965015, ECO:0007744|PDB:2QPP

Chain	Residue	Details
A	GLY183
D	GLY183
D	GLU228
D	GLN232
A	GLU228
A	GLN232
B	GLY183
B	GLU228
B	GLN232
C	GLY183
C	GLU228
C	GLN232

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P09601

Chain	Residue	Details
A	PHE189
B	PHE189
C	PHE189
D	PHE189

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ALA31
B	ALA31
C	ALA31
D	ALA31

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