Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3BK9

H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
A	0006569	biological_process	tryptophan catabolic process
A	0019441	biological_process	tryptophan catabolic process to kynurenine
A	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
B	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
B	0006569	biological_process	tryptophan catabolic process
B	0019441	biological_process	tryptophan catabolic process to kynurenine
B	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
C	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
C	0006569	biological_process	tryptophan catabolic process
C	0019441	biological_process	tryptophan catabolic process to kynurenine
C	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
D	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
D	0006569	biological_process	tryptophan catabolic process
D	0019441	biological_process	tryptophan catabolic process to kynurenine
D	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
E	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
E	0006569	biological_process	tryptophan catabolic process
E	0019441	biological_process	tryptophan catabolic process to kynurenine
E	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
F	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
F	0006569	biological_process	tryptophan catabolic process
F	0019441	biological_process	tryptophan catabolic process to kynurenine
F	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity
G	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
G	0006569	biological_process	tryptophan catabolic process
G	0019441	biological_process	tryptophan catabolic process to kynurenine
G	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
G	0020037	molecular_function	heme binding
G	0046872	molecular_function	metal ion binding
G	0051213	molecular_function	dioxygenase activity
H	0004833	molecular_function	tryptophan 2,3-dioxygenase activity
H	0006569	biological_process	tryptophan catabolic process
H	0019441	biological_process	tryptophan catabolic process to kynurenine
H	0019442	biological_process	tryptophan catabolic process to acetyl-CoA
H	0020037	molecular_function	heme binding
H	0046872	molecular_function	metal ion binding
H	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRP A 402

Chain	Residue
A	PHE51
A	HOH793
A	TYR113
A	ARG117
A	SER123
A	SER124
A	GLY253
A	THR254
A	HEM401
A	HOH552

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRP B 402

Chain	Residue
A	TYR24
B	PHE51
B	TYR113
B	ARG117
B	SER123
B	SER124
B	GLY253
B	THR254
B	HEM401
B	HOH602

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRP C 402

Chain	Residue
C	PHE51
C	TYR113
C	ARG117
C	SER123
C	SER124
C	ILE248
C	GLY253
C	THR254
C	HEM401
D	TYR24

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRP D 402

Chain	Residue
C	TYR24
D	PHE51
D	TYR113
D	ARG117
D	SER123
D	SER124
D	GLY253
D	THR254
D	HEM401
D	HOH621

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRP E 402

Chain	Residue
E	PHE51
E	TYR113
E	ARG117
E	SER123
E	SER124
E	GLY253
E	THR254
E	HEM401
E	HOH642
F	TYR24
F	TYR27

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRP F 402

Chain	Residue
F	PHE51
F	TYR113
F	ARG117
F	SER123
F	SER124
F	GLY253
F	THR254
F	HEM401
F	HOH662

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRP G 402

Chain	Residue
G	PHE51
G	TYR113
G	ARG117
G	SER123
G	SER124
G	GLY253
G	THR254
G	HEM401
G	HOH663
H	TYR27
H	LEU28

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRP H 402

Chain	Residue
H	PHE51
H	TYR113
H	ARG117
H	LEU120
H	SER123
H	SER124
H	ILE248
H	GLY253
H	THR254
H	HEM401
H	HOH1542

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 401

Chain	Residue
B	TYR24
A	GLN54
A	TRP102
A	SER124
A	GLY125
A	PHE126
A	TYR131
A	ARG132
A	HIS240
A	VAL244
A	GLY253
A	GLY255
A	GLY256
A	SER257
A	TRP402
A	HOH552
A	HOH627
B	ARG8

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRP D 403

Chain	Residue
A	LYS86
D	ARG85
D	LYS92
D	SER221
D	ASP225
D	ASP228
D	HOH504
D	HOH813
D	HOH821

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B 401

Chain	Residue
A	ARG8
B	SER58
B	TRP102
B	LEU105
B	SER124
B	GLY125
B	PHE126
B	TYR131
B	ARG132
B	TRP236
B	HIS240
B	VAL244
B	GLY253
B	THR254
B	GLY255
B	GLY256
B	SER257
B	LEU263
B	ALA266
B	TRP402
B	HOH700
B	HOH1541

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRP C 403

Chain	Residue
B	LYS86
C	ARG85
C	LYS92
C	TYR220
C	SER221
C	ASP228
C	HOH521
C	HOH912
C	HOH932
C	HOH1094

site_id	BC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 401

Chain	Residue
C	GLN54
C	TRP102
C	SER124
C	GLY125
C	PHE126
C	TYR131
C	ARG132
C	TRP236
C	HIS240
C	VAL244
C	GLY253
C	GLY255
C	SER257
C	TRP402
C	HOH632
C	HOH1308
D	TYR24

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRP B 403

Chain	Residue
B	ARG85
B	LYS92
B	SER221
B	GLU224
B	ASP228
B	HOH545
B	HOH644
B	HOH718
C	LYS86

site_id	BC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM D 401

Chain	Residue
C	ARG8
C	TYR24
D	GLN54
D	SER58
D	TRP102
D	LEU105
D	SER124
D	GLY125
D	PHE126
D	TYR131
D	ARG132
D	HIS240
D	VAL244
D	VAL247
D	GLY253
D	GLY255
D	GLY256
D	SER257
D	GLY259
D	LEU263
D	ALA266
D	TRP402
D	HOH621

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRP A 403

Chain	Residue
A	ARG85
A	LYS92
A	SER221
A	GLU224
A	ASP225
A	ASP228
A	HOH537
A	HOH788
A	HOH1313
A	HOH1475
D	LYS86

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM E 401

Chain	Residue
E	PHE51
E	GLN54
E	TRP102
E	SER124
E	GLY125
E	PHE126
E	TYR131
E	ARG132
E	HIS240
E	VAL244
E	GLY253
E	THR254
E	GLY255
E	SER257
E	GLY259
E	TRP402
E	HOH642
E	HOH798
F	TYR24

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRP E 403

Chain	Residue
E	ARG85
E	LYS92
E	SER221
E	ASP228
G	LYS86
G	ALA89

site_id	CC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM F 401

Chain	Residue
E	TYR24
F	GLN54
F	SER58
F	TRP102
F	SER124
F	GLY125
F	PHE126
F	TYR131
F	ARG132
F	TRP236
F	HIS240
F	VAL244
F	VAL247
F	GLY253
F	GLY255
F	GLY256
F	SER257
F	GLY259
F	LEU263
F	TRP402
F	HOH662

site_id	CC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM G 401

Chain	Residue
G	GLN54
G	SER58
G	TRP102
G	SER124
G	GLY125
G	PHE126
G	TYR131
G	ARG132
G	HIS240
G	VAL244
G	VAL247
G	ILE248
G	GLY253
G	GLY255
G	GLY256
G	SER257
G	LEU263
G	TRP402
G	HOH663
G	HOH1133
G	HOH1411

site_id	CC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM H 401

Chain	Residue
G	TYR24
H	GLN54
H	ALA55
H	SER58
H	TRP102
H	SER124
H	GLY125
H	PHE126
H	TYR131
H	ARG132
H	TRP236
H	HIS240
H	VAL244
H	VAL247
H	GLY253
H	GLY255
H	GLY256
H	SER257
H	GLY259
H	TRP402
H	HOH1542

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01972, ECO:0000269\|PubMed:17197414, ECO:0000269\|PubMed:18783250, ECO:0007744\|PDB:2NW8, ECO:0007744\|PDB:3BK9

Chain	Residue	Details
A	PHE51
B	PHE51
C	PHE51
D	PHE51
E	PHE51
F	PHE51
G	PHE51
H	PHE51

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01972, ECO:0000269\|PubMed:17197414, ECO:0000269\|PubMed:18783250, ECO:0007744\|PDB:2NW8, ECO:0007744\|PDB:3BK9, ECO:0007744\|PDB:3E08

Chain	Residue	Details
A	TYR113
A	ARG117
A	THR254
B	TYR113
B	ARG117
B	THR254
C	TYR113
C	ARG117
C	THR254
D	TYR113
D	ARG117
D	THR254
E	TYR113
E	ARG117
E	THR254
F	TYR113
F	ARG117
F	THR254
G	TYR113
G	ARG117
G	THR254
H	TYR113
H	ARG117
H	THR254

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: axial binding residue => ECO:0000255\|HAMAP-Rule:MF_01972, ECO:0000269\|PubMed:17197414, ECO:0000269\|PubMed:18783250, ECO:0007744\|PDB:2NW7, ECO:0007744\|PDB:2NW8, ECO:0007744\|PDB:2NW9, ECO:0007744\|PDB:3BK9, ECO:0007744\|PDB:3E08

Chain	Residue	Details
A	HIS240
B	HIS240
C	HIS240
D	HIS240
E	HIS240
F	HIS240
G	HIS240
H	HIS240

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