4MEC

Crystal structure of RAT Heme oxygenase-1 in complex with ZN(II)-Protoporphyrin IX

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
E	0004392	molecular_function	heme oxygenase (decyclizing) activity
E	0006788	biological_process	heme oxidation
F	0004392	molecular_function	heme oxygenase (decyclizing) activity
F	0006788	biological_process	heme oxidation
G	0004392	molecular_function	heme oxygenase (decyclizing) activity
G	0006788	biological_process	heme oxidation

Functional Information from PDB Data

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

Chain	Residue
A	LYS18
A	LEU147
A	ARG183
A	PHE207
B	GLN70
A	HIS25
A	GLU29
A	TYR134
A	THR135
A	ARG136
A	GLY139
A	SER142
A	GLY143

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ZNH B 300

Chain	Residue
B	HIS25
B	GLU29
B	MET34
B	GLN38
B	TYR134
B	THR135
B	ARG136
B	GLY139
B	SER142
B	GLY143
B	LEU147
B	LYS179
B	ARG183
B	PHE207
B	ASN210
C	LYS69
C	GLN70

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZNH C 300

Chain	Residue
C	HIS25
C	GLN38
C	THR135
C	ARG136
C	GLY139
C	SER142

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ZNH D 300

Chain	Residue
C	THR222
D	HIS25
D	GLU29
D	TYR134
D	THR135
D	ARG136
D	LEU138
D	PHE207

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ZNH E 300

Chain	Residue
E	HIS25
E	GLU29
E	GLN38
E	TYR134
E	THR135
E	GLY143
E	PHE207
E	ASN210

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZNH F 300

Chain	Residue
F	HIS25
F	SER142
F	GLY143

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZNH G 300

Chain	Residue
G	HIS25

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P09601

Chain	Residue	Details
A	LYS18
D	LYS18
D	TYR134
D	ARG183
E	LYS18
E	TYR134
E	ARG183
F	LYS18
F	TYR134
F	ARG183
G	LYS18
A	TYR134
G	TYR134
G	ARG183
A	ARG183
B	LYS18
B	TYR134
B	ARG183
C	LYS18
C	TYR134
C	ARG183

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: axial binding residue => ECO:0000250|UniProtKB:P09601

Chain	Residue	Details
A	HIS25
B	HIS25
C	HIS25
D	HIS25
E	HIS25
F	HIS25
G	HIS25

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P09601

Chain	Residue	Details
A	ASP140
B	ASP140
C	ASP140
D	ASP140
E	ASP140
F	ASP140
G	ASP140

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09601

Chain	Residue	Details
A	SER229
B	SER229
C	SER229
D	SER229
E	SER229
F	SER229
G	SER229

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