Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RIM

Crystal structure of mycobacterium tuberculosis Transketolase (Rv1449c)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004802	molecular_function	transketolase activity
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006098	biological_process	pentose-phosphate shunt
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016740	molecular_function	transferase activity
A	0016744	molecular_function	transketolase or transaldolase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004802	molecular_function	transketolase activity
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006098	biological_process	pentose-phosphate shunt
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016740	molecular_function	transferase activity
B	0016744	molecular_function	transketolase or transaldolase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004802	molecular_function	transketolase activity
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006098	biological_process	pentose-phosphate shunt
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016740	molecular_function	transferase activity
C	0016744	molecular_function	transketolase or transaldolase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004802	molecular_function	transketolase activity
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006098	biological_process	pentose-phosphate shunt
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016740	molecular_function	transferase activity
D	0016744	molecular_function	transketolase or transaldolase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1001

Chain	Residue
A	ASP177
A	ASN207
A	ILE209
A	HOH779
A	TPP1002

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE TPP A 1002

Chain	Residue
A	SER176
A	ASP177
A	GLY178
A	GLU182
A	ASN207
A	ILE209
A	SER210
A	ILE211
A	HIS283
A	HOH779
A	MG1001
C	ASP401
C	GLU441
C	PHE467
C	TYR470
C	HIS503
C	HOH748
A	THR48
A	HIS85
A	GLY133
A	LEU135

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1001

Chain	Residue
B	ASP177
B	ASN207
B	ILE209
B	HOH819
B	TPP1002

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE TPP B 1002

Chain	Residue
B	THR48
B	HIS85
B	GLY133
B	LEU135
B	SER176
B	ASP177
B	GLY178
B	GLU182
B	ASN207
B	ILE209
B	SER210
B	ILE211
B	ILE269
B	HIS283
B	HOH819
B	MG1001
D	ASP401
D	GLU441
D	PHE467
D	TYR470
D	HIS503
D	HOH811

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 701

Chain	Residue
B	ILE7
B	SER8
B	ALA9

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 702

Chain	Residue
B	CYS220
D	TYR230
D	GLY231

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1001

Chain	Residue
C	ASP177
C	ASN207
C	ILE209
C	HOH760
C	TPP1002

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE TPP C 1002

Chain	Residue
A	ASP401
A	GLU441
A	PHE467
A	TYR470
A	HIS503
C	THR48
C	HIS85
C	GLY133
C	PRO134
C	LEU135
C	SER176
C	ASP177
C	GLY178
C	GLU182
C	ASN207
C	ILE209
C	SER210
C	ILE269
C	HIS283
C	HOH747
C	HOH760
C	MG1001

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 701

Chain	Residue
C	TRP430
C	TYR431

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 702

Chain	Residue
B	HIS15
B	HOH830
C	ARG123

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1001

Chain	Residue
D	ASP177
D	ASN207
D	ILE209
D	HOH838
D	TPP1002

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP D 1002

Chain	Residue
B	PHE467
B	TYR470
B	HIS503
D	THR48
D	HIS85
D	GLY133
D	LEU135
D	SER176
D	ASP177
D	GLY178
D	GLU182
D	ASN207
D	ILE209
D	SER210
D	ILE269
D	HIS283
D	HOH738
D	HOH838
D	HOH840
D	MG1001
B	ASP401
B	VAL439
B	GLU441

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 701

Chain	Residue
D	ARG378
D	SER405
D	HIS491
D	ARG552

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 702

Chain	Residue
D	ALA403
D	ASN407
D	THR409
D	TYR426

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 703

Chain	Residue
B	ARG351
B	LYS356
D	ASP17
D	TYR18

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 704

Chain	Residue
D	PHE122
D	VAL452
D	ASP484

Functional Information from PROSITE/UniProt

site_id	PS00801
Number of Residues	21
Details	TRANSKETOLASE_1 Transketolase signature 1. RvlaADavqkvgNGHPGtaMS

Chain	Residue	Details
A	ARG31-SER51

site_id	PS00802
Number of Residues	17
Details	TRANSKETOLASE_2 Transketolase signature 2. GEDGPTHqPIEhlSalR

Chain	Residue	Details
A	GLY497-ARG513

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305

Chain	Residue	Details
B	GLU441
A	GLU441
C	GLU441
D	GLU441

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ARG378
A	ASP499
A	ARG552
B	HIS45
B	ARG378
B	SER405
B	HIS491
B	ASP499
B	ARG552
C	HIS45
C	ARG378
C	SER405
C	HIS491
C	ASP499
C	ARG552
D	HIS45
D	ARG378
D	SER405
D	HIS491
D	ASP499
D	ARG552
A	HIS45
A	SER405
A	HIS491

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING:

Chain	Residue	Details
A	GLY133
B	THR48
B	HIS85
B	GLY133
B	LEU135
B	GLY178
B	ASN207
B	HIS283
B	PHE467
C	THR48
C	HIS85
C	GLY133
C	LEU135
C	GLY178
C	ASN207
C	HIS283
C	PHE467
D	THR48
D	HIS85
D	GLY133
D	LEU135
D	GLY178
D	ASN207
D	HIS283
D	PHE467
A	THR48
A	HIS85
A	LEU135
A	GLY178
A	ASN207
A	HIS283
A	PHE467

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:22645655

Chain	Residue	Details
C	ASP177
C	ILE209
D	ASP177
D	ILE209
A	ASP177
A	ILE209
B	ASP177
B	ILE209

site_id	SWS_FT_FI5
Number of Residues	8
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
C	HIS45
C	HIS283
A	HIS45
A	HIS283
B	HIS45
B	HIS283
D	HIS45
D	HIS283

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N-acetylthreonine => ECO:0007744\|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2

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