1OZR

Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM A 300

Chain	Residue
A	LYS18
A	ARG183
A	PHE207
A	ASN210
A	HOH363
A	HIS25
A	GLU29
A	TYR134
A	THR135
A	ARG136
A	GLY139
A	SER142
A	GLY143

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HEM B 300

Chain	Residue
B	LYS18
B	HIS25
B	TYR134
B	ARG136
B	GLY139
B	ARG183
B	PHE207
B	ASN210
B	HOH374

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU129-GLY139

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW

Chain	Residue	Details
A	ARG183
B	LYS18
B	TYR134
B	ARG183
A	LYS18
A	TYR134

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:12842469, ECO:0007744|PDB:1OZW

Chain	Residue	Details
A	HIS25
B	HIS25

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000269|PubMed:11121422

Chain	Residue	Details
A	ASP140
B	ASP140

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER229
B	SER229

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