Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OS7

Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000908	molecular_function	taurine dioxygenase activity
A	0005737	cellular_component	cytoplasm
A	0006790	biological_process	sulfur compound metabolic process
A	0008198	molecular_function	ferrous iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
A	0019529	biological_process	taurine catabolic process
A	0031418	molecular_function	L-ascorbic acid binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051289	biological_process	protein homotetramerization
A	1990205	cellular_component	taurine dioxygenase complex
B	0000908	molecular_function	taurine dioxygenase activity
B	0005737	cellular_component	cytoplasm
B	0006790	biological_process	sulfur compound metabolic process
B	0008198	molecular_function	ferrous iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
B	0019529	biological_process	taurine catabolic process
B	0031418	molecular_function	L-ascorbic acid binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	0051289	biological_process	protein homotetramerization
B	1990205	cellular_component	taurine dioxygenase complex
C	0000908	molecular_function	taurine dioxygenase activity
C	0005737	cellular_component	cytoplasm
C	0006790	biological_process	sulfur compound metabolic process
C	0008198	molecular_function	ferrous iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
C	0019529	biological_process	taurine catabolic process
C	0031418	molecular_function	L-ascorbic acid binding
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051289	biological_process	protein homotetramerization
C	1990205	cellular_component	taurine dioxygenase complex
D	0000908	molecular_function	taurine dioxygenase activity
D	0005737	cellular_component	cytoplasm
D	0006790	biological_process	sulfur compound metabolic process
D	0008198	molecular_function	ferrous iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
D	0019529	biological_process	taurine catabolic process
D	0031418	molecular_function	L-ascorbic acid binding
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0051289	biological_process	protein homotetramerization
D	1990205	cellular_component	taurine dioxygenase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 A 302

Chain	Residue
A	HIS99
A	ASP101
A	HIS255
A	AKG501

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 B 302

Chain	Residue
B	HIS99
B	ASP101
B	HIS255
B	AKG502

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 C 302

Chain	Residue
C	ASP101
C	HIS255
C	AKG503
C	HIS99

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 D 302

Chain	Residue
D	HIS99
D	ASP101
D	HIS255
D	AKG504

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TAU A 401

Chain	Residue
A	HIS70
A	ASN95
A	ASP101
A	VAL102
A	PHE159
A	PHE206
A	ARG270
A	HOH540

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AKG A 501

Chain	Residue
A	LEU85
A	ASN95
A	HIS99
A	ASP101
A	LEU114
A	THR126
A	TRP240
A	HIS255
A	ARG266
A	MET268
A	ARG270
A	FE2302
A	HOH546

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TAU B 402

Chain	Residue
B	HIS70
B	TYR73
B	ASP94
B	ASN95
B	HIS99
B	VAL102
B	PHE159
B	PHE206
B	ARG270

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AKG B 502

Chain	Residue
B	ASN95
B	HIS99
B	ASP101
B	LEU114
B	THR126
B	TRP240
B	HIS255
B	ARG266
B	ARG270
B	FE2302

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAU C 403

Chain	Residue
C	HIS70
C	TYR73
C	ASN95
C	HIS99
C	ASP101
C	VAL102
C	PHE104
C	PHE159
C	PHE206
C	ARG270
C	HOH565

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AKG C 503

Chain	Residue
C	LEU85
C	ASN95
C	HIS99
C	ASP101
C	LEU114
C	THR126
C	TRP240
C	HIS255
C	ALA257
C	ARG266
C	ARG270
C	FE2302

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AKG D 504

Chain	Residue
D	ASN95
D	HIS99
D	ASP101
D	LEU114
D	THR126
D	HIS255
D	ARG266
D	ARG270
D	FE2302
D	HOH602

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:11955067, ECO:0000269\|PubMed:12741810

Chain	Residue	Details
A	PRO71
A	ALA271
B	PRO71
B	PRO74
B	ASP96
B	THR100
B	VAL102
B	THR103
B	LEU127
B	TYR256
B	ILE267
A	PRO74
B	ALA271
C	PRO71
C	PRO74
C	ASP96
C	THR100
C	VAL102
C	THR103
C	LEU127
C	TYR256
C	ILE267
A	ASP96
C	ALA271
D	PRO71
D	PRO74
D	ASP96
D	THR100
D	VAL102
D	THR103
D	LEU127
D	TYR256
D	ILE267
A	THR100
D	ALA271
A	VAL102
A	THR103
A	LEU127
A	TYR256
A	ILE267

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: 3-hydroxytryptophan; by autocatalysis => ECO:0000269\|PubMed:11955067

Chain	Residue	Details
A	THR129
D	THR129
D	GLN241
D	ASP249
A	GLN241
A	ASP249
B	THR129
B	GLN241
B	ASP249
C	THR129
C	GLN241
C	ASP249

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15924433, 15023059

Chain	Residue	Details
A	ARG270

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15924433, 15023059

Chain	Residue	Details
B	ARG270

site_id	CSA3
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15924433, 15023059

Chain	Residue	Details
C	ARG270

site_id	CSA4
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15924433, 15023059

Chain	Residue	Details
D	ARG270

site_id	MCSA1
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
A	HIS99	metal ligand
A	ASP101	metal ligand
A	HIS255	metal ligand
A	ARG270	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
B	HIS99	metal ligand
B	ASP101	metal ligand
B	HIS255	metal ligand
B	ARG270	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
C	HIS99	metal ligand
C	ASP101	metal ligand
C	HIS255	metal ligand
C	ARG270	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
D	HIS99	metal ligand
D	ASP101	metal ligand
D	HIS255	metal ligand
D	ARG270	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)