1DQI

CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE FROM P. FURIOSUS IN THE OXIDIZED STATE AT 1.7 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0050605	molecular_function	superoxide reductase activity
A	0098869	biological_process	cellular oxidant detoxification
B	0005506	molecular_function	iron ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0050605	molecular_function	superoxide reductase activity
B	0098869	biological_process	cellular oxidant detoxification
C	0005506	molecular_function	iron ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0050605	molecular_function	superoxide reductase activity
C	0098869	biological_process	cellular oxidant detoxification
D	0005506	molecular_function	iron ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0050605	molecular_function	superoxide reductase activity
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE A 501

Chain	Residue
A	GLU14
A	HIS16
A	HIS41
A	HIS47
A	CYS111
A	HIS114

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE B 502

Chain	Residue
B	CYS111
B	HIS114
B	HOH536
B	HIS16
B	HIS41
B	HIS47

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE C 503

Chain	Residue
C	GLU14
C	HIS16
C	HIS41
C	HIS47
C	CYS111
C	HIS114

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE D 504

Chain	Residue
D	HIS16
D	HIS41
D	HIS47
D	CYS111
D	HIS114
D	HOH568

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1do6

Chain	Residue	Details
A	LYS15
A	GLU14

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1do6

Chain	Residue	Details
B	LYS15
B	GLU14

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1do6

Chain	Residue	Details
C	LYS15
C	GLU14

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1do6

Chain	Residue	Details
D	LYS15
D	GLU14

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site_id	MCSA1
Number of Residues	7
Details	M-CSA 660

Chain	Residue	Details
A	GLU14	electrostatic stabiliser, metal ligand, nucleophile
A	LYS15	proton donor
A	HIS16	metal ligand
A	HIS41	metal ligand
A	HIS47	metal ligand
A	CYS111	metal ligand
A	HIS114	metal ligand

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 660

Chain	Residue	Details
B	GLU14	electrostatic stabiliser, metal ligand, nucleophile
B	LYS15	proton donor
B	HIS16	metal ligand
B	HIS41	metal ligand
B	HIS47	metal ligand
B	CYS111	metal ligand
B	HIS114	metal ligand

---

site_id	MCSA3
Number of Residues	7
Details	M-CSA 660

Chain	Residue	Details
C	GLU14	electrostatic stabiliser, metal ligand, nucleophile
C	LYS15	proton donor
C	HIS16	metal ligand
C	HIS41	metal ligand
C	HIS47	metal ligand
C	CYS111	metal ligand
C	HIS114	metal ligand

---

site_id	MCSA4
Number of Residues	7
Details	M-CSA 660

Chain	Residue	Details
D	GLU14	electrostatic stabiliser, metal ligand, nucleophile
D	LYS15	proton donor
D	HIS16	metal ligand
D	HIS41	metal ligand
D	HIS47	metal ligand
D	CYS111	metal ligand
D	HIS114	metal ligand

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