Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VVP

Crystal structure of Mycobacterium tuberculosis ribose-5-phosphate isomerase B in complex with its substrates ribose 5-phosphate and ribulose 5-phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004751	molecular_function	ribose-5-phosphate isomerase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
A	0016853	molecular_function	isomerase activity
A	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
A	0019316	biological_process	D-allose catabolic process
B	0004751	molecular_function	ribose-5-phosphate isomerase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0006098	biological_process	pentose-phosphate shunt
B	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
B	0016853	molecular_function	isomerase activity
B	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
B	0019316	biological_process	D-allose catabolic process
C	0004751	molecular_function	ribose-5-phosphate isomerase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005975	biological_process	carbohydrate metabolic process
C	0006098	biological_process	pentose-phosphate shunt
C	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
C	0016853	molecular_function	isomerase activity
C	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
C	0019316	biological_process	D-allose catabolic process
D	0004751	molecular_function	ribose-5-phosphate isomerase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005975	biological_process	carbohydrate metabolic process
D	0006098	biological_process	pentose-phosphate shunt
D	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
D	0016853	molecular_function	isomerase activity
D	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
D	0019316	biological_process	D-allose catabolic process
E	0004751	molecular_function	ribose-5-phosphate isomerase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005975	biological_process	carbohydrate metabolic process
E	0006098	biological_process	pentose-phosphate shunt
E	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
E	0016853	molecular_function	isomerase activity
E	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
E	0019316	biological_process	D-allose catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE R52 A 200

Chain	Residue
A	ASP11
A	HOH2188
A	HOH2189
A	HOH2190
A	HOH2191
A	HOH2192
B	HIS102
B	ASN103
B	ARG137
B	ARG141
A	HIS12
A	ALA13
A	GLY69
A	GLY70
A	SER71
A	GLY74
A	GLU75
A	ARG113

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 5RP A 300

Chain	Residue
A	ASP11
A	HIS12
A	GLY70
A	SER71
A	GLY72
A	ASN73
A	GLY74
A	GLU75
A	ARG113
A	HOH2188
A	HOH2190
A	HOH2191
A	HOH2192
B	HIS102
B	ASN103
B	ARG137
B	ARG141

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE R52 B 200

Chain	Residue
A	HIS102
A	ASN103
A	ARG137
A	ARG141
B	ASP11
B	HIS12
B	ALA13
B	GLY69
B	GLY70
B	SER71
B	GLY74
B	GLU75
B	ARG113
B	HOH2197
B	HOH2198
B	HOH2199
B	HOH2200
B	HOH2201

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 5RP B 300

Chain	Residue
A	HIS102
A	ASN103
A	ARG137
A	ARG141
B	ASP11
B	HIS12
B	ALA13
B	GLY69
B	GLY70
B	SER71
B	ASN73
B	GLY74
B	GLU75
B	ARG113
B	HOH2197
B	HOH2198
B	HOH2200
B	HOH2201

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE R52 C 200

Chain	Residue
C	ASP11
C	HIS12
C	ALA13
C	GLY70
C	SER71
C	GLY74
C	GLU75
C	ARG113
C	HOH2202
C	HOH2203
C	HOH2204
C	HOH2205
C	HOH2206
D	HIS102
D	ASN103
D	ARG137
D	ARG141

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 5RP C 300

Chain	Residue
C	HOH2202
C	HOH2203
C	HOH2205
C	HOH2206
D	HIS102
D	ASN103
D	ARG137
D	ARG141
C	ASP11
C	HIS12
C	ALA13
C	GLY69
C	GLY70
C	SER71
C	GLY72
C	ASN73
C	GLY74
C	GLU75
C	ARG113

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE R52 D 200

Chain	Residue
C	HIS102
C	ASN103
C	ARG137
C	ARG141
D	ASP11
D	HIS12
D	ALA13
D	GLY69
D	GLY70
D	SER71
D	GLY74
D	GLU75
D	ARG113
D	HOH2199
D	HOH2200
D	HOH2201
D	HOH2202

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 5RP D 300

Chain	Residue
C	HIS102
C	ASN103
C	ARG137
C	ARG141
D	ASP11
D	HIS12
D	ALA13
D	GLY70
D	SER71
D	GLY74
D	GLU75
D	ARG113
D	HOH2199
D	HOH2201
D	HOH2202
D	HOH2203

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE R52 E 200

Chain	Residue
D	HOH2158
E	ASP11
E	HIS12
E	ALA13
E	GLY69
E	GLY70
E	SER71
E	ASN73
E	GLY74
E	GLU75
E	HIS102
E	ASN103
E	ARG113
E	ARG137
E	ARG141
E	HOH2177
E	HOH2178
E	HOH2179
E	HOH2180

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 5RP E 300

Chain	Residue
D	HOH2158
E	ASP11
E	HIS12
E	ALA13
E	GLY70
E	SER71
E	GLY74
E	GLU75
E	HIS102
E	ASN103
E	ARG113
E	ARG137
E	ARG141
E	HOH2178
E	HOH2179
E	HOH2180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:15590681, ECO:0000305\|PubMed:18640127, ECO:0007744\|PDB:2BES, ECO:0007744\|PDB:2BET, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP, ECO:0007744\|PDB:2VVQ

Chain	Residue	Details
A	GLU75
B	GLU75
C	GLU75
D	GLU75
E	GLU75

site_id	SWS_FT_FI2
Number of Residues	5
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:15590681, ECO:0000305\|PubMed:18640127, ECO:0007744\|PDB:2BES, ECO:0007744\|PDB:2BET, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP, ECO:0007744\|PDB:2VVQ

Chain	Residue	Details
A	HIS102
B	HIS102
C	HIS102
D	HIS102
E	HIS102

site_id	SWS_FT_FI3
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269\|PubMed:14687575, ECO:0000269\|PubMed:15590681, ECO:0000269\|PubMed:18640127, ECO:0007744\|PDB:1USL, ECO:0007744\|PDB:2BES, ECO:0007744\|PDB:2BET, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP, ECO:0007744\|PDB:2VVQ

Chain	Residue	Details
B	ARG137
C	ASP11
C	ARG113
C	ARG137
D	ASP11
D	ARG113
D	ARG137
E	ASP11
E	ARG113
E	ARG137
A	ASP11
A	ARG113
A	ARG137
B	ASP11
B	ARG113

site_id	SWS_FT_FI4
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:15590681, ECO:0000269\|PubMed:18640127, ECO:0007744\|PDB:2BES, ECO:0007744\|PDB:2BET, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP, ECO:0007744\|PDB:2VVQ

Chain	Residue	Details
A	GLY70
B	GLY70
C	GLY70
D	GLY70
E	GLY70

site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:15590681, ECO:0000269\|PubMed:18640127, ECO:0007744\|PDB:2BET, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP

Chain	Residue	Details
A	ASN103
B	ASN103
C	ASN103
D	ASN103
E	ASN103

site_id	SWS_FT_FI6
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:14687575, ECO:0000269\|PubMed:18640127, ECO:0007744\|PDB:1USL, ECO:0007744\|PDB:2VVO, ECO:0007744\|PDB:2VVP, ECO:0007744\|PDB:2VVQ

Chain	Residue	Details
A	ARG141
B	ARG141
C	ARG141
D	ARG141
E	ARG141

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