5UCA

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

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 PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue DAO B 301

Chain	Residue
B	GLU49
B	LEU74
B	ARG156
B	TYR187
B	PHE234

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site_id	AC2
Number of Residues	4
Details	binding site for residue DAO C 301

Chain	Residue
C	GLU49
C	VAL54
C	LEU74
C	ARG156

---

site_id	AC3
Number of Residues	8
Details	binding site for residue DAO D 301

Chain	Residue
D	VAL54
D	ALA70
D	THR77
D	ARG156
D	TYR187
D	ASN230
D	PHE234
D	HOH404

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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 site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"17965015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QPP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17965015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QPP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P09601","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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