4J5I

Crystal structure of an alpha-ketoglutarate-dependent taurine dioxygenase from Mycobacterium smegmatis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000908	molecular_function	taurine dioxygenase activity
A	0005737	cellular_component	cytoplasm
A	0016491	molecular_function	oxidoreductase activity
A	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
B	0000908	molecular_function	taurine dioxygenase activity
B	0005737	cellular_component	cytoplasm
B	0016491	molecular_function	oxidoreductase activity
B	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
C	0000908	molecular_function	taurine dioxygenase activity
C	0005737	cellular_component	cytoplasm
C	0016491	molecular_function	oxidoreductase activity
C	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
D	0000908	molecular_function	taurine dioxygenase activity
D	0005737	cellular_component	cytoplasm
D	0016491	molecular_function	oxidoreductase activity
D	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
E	0000908	molecular_function	taurine dioxygenase activity
E	0005737	cellular_component	cytoplasm
E	0016491	molecular_function	oxidoreductase activity
E	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
F	0000908	molecular_function	taurine dioxygenase activity
F	0005737	cellular_component	cytoplasm
F	0016491	molecular_function	oxidoreductase activity
F	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity
G	0000908	molecular_function	taurine dioxygenase activity
G	0005737	cellular_component	cytoplasm
G	0016491	molecular_function	oxidoreductase activity
G	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
G	0046872	molecular_function	metal ion binding
G	0051213	molecular_function	dioxygenase activity
H	0000908	molecular_function	taurine dioxygenase activity
H	0005737	cellular_component	cytoplasm
H	0016491	molecular_function	oxidoreductase activity
H	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
H	0046872	molecular_function	metal ion binding
H	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 401

Chain	Residue
A	HIS95
A	ASP97
A	HIS248
A	HOH532

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 402

Chain	Residue
A	ASP220
A	ARG221
A	ARG224
B	HOH509

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 401

Chain	Residue
B	ASP97
B	HIS248
B	ARG263
B	HOH580
B	HIS95

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE C 401

Chain	Residue
C	HIS95
C	ASP97
C	HIS248
C	ARG263

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 401

Chain	Residue
D	HIS95
D	ASP97
D	HIS248
D	ARG263

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 401

Chain	Residue
E	HIS95
E	ASP97
E	HIS248
E	ARG263
E	HOH564

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE F 401

Chain	Residue
F	HIS95
F	ASP97
F	HIS248
F	ARG263
F	HOH561

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 402

Chain	Residue
F	GLU62
F	GLY65
F	HOH538
F	HOH539

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site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE G 401

Chain	Residue
G	HIS95
G	ASP97
G	HIS248
G	ARG263

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE H 401

Chain	Residue
H	HIS95
H	ASP97
H	HIS248
H	ARG263
H	HOH553
H	HOH554

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