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 |
A | ASP11 | |
D | ASP11 | |
D | ARG113 | |
D | ARG137 | |
E | ASP11 | |
E | ARG113 | |
E | ARG137 | |
A | ARG113 | |
A | ARG137 | |
B | ASP11 | |
B | ARG113 | |
B | ARG137 | |
C | ASP11 | |
C | ARG113 | |
C | ARG137 |
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 |