Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OTJ

Crystal structure of APO (iron-free) TauD

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	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	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	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	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	2
Details	BINDING SITE FOR RESIDUE CL A 900

Chain	Residue
A	LEU114
A	ARG266

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 901

Chain	Residue
B	LEU114
B	THR126
B	ARG266
B	HOH1064

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 902

Chain	Residue
D	LEU114
D	THR126
D	ARG266

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAU A 952

Chain	Residue
A	HIS70
A	TYR73
A	ASN95
A	ASP101
A	VAL102
A	PHE104
A	PHE159
A	PHE206
A	ARG270
A	HOH972
A	HOH1017

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TAU B 953

Chain	Residue
B	HIS70
B	TYR73
B	ASN95
B	HIS99
B	ASP101
B	VAL102
B	PHE159
B	ARG270
B	HOH995

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAU C 954

Chain	Residue
C	HIS70
C	TYR73
C	ASN95
C	HIS99
C	ASP101
C	VAL102
C	PHE159
C	PHE206
C	ARG270
C	HOH981
C	HOH1100

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	MCSA1
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
A	THR100	metal ligand
A	VAL102	metal ligand
A	TYR256	metal ligand
A	ALA271	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
B	THR100	metal ligand
B	VAL102	metal ligand
B	TYR256	metal ligand
B	ALA271	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
C	THR100	metal ligand
C	VAL102	metal ligand
C	TYR256	metal ligand
C	ALA271	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 129

Chain	Residue	Details
D	THR100	metal ligand
D	VAL102	metal ligand
D	TYR256	metal ligand
D	ALA271	electrostatic stabiliser, hydrogen bond donor

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