2VVQ
Crystal structure of Mycobacterium tuberculosis ribose-5-phosphate isomerase B in complex with the inhibitor 5-deoxy-5-phospho-D- ribonate
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 | 20 |
| Details | BINDING SITE FOR RESIDUE R10 A 200 |
| Chain | Residue |
| A | ASP11 |
| A | GLU75 |
| A | ARG113 |
| A | HOH2033 |
| A | HOH2107 |
| A | HOH2108 |
| A | HOH2109 |
| B | HIS102 |
| B | ASN103 |
| B | ARG137 |
| B | ARG141 |
| A | HIS12 |
| C | HOH2084 |
| A | TYR46 |
| A | GLY69 |
| A | GLY70 |
| A | SER71 |
| A | GLY72 |
| A | ASN73 |
| A | GLY74 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 300 |
| Chain | Residue |
| A | HOH2110 |
| A | HOH2111 |
| A | HOH2112 |
| B | HIS152 |
| D | ARG5 |
| D | HOH2046 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE R10 B 200 |
| Chain | Residue |
| A | HIS102 |
| A | ASN103 |
| A | ARG137 |
| A | ARG141 |
| A | HOH2084 |
| B | ASP11 |
| B | HIS12 |
| B | TYR46 |
| B | GLY69 |
| B | GLY70 |
| B | SER71 |
| B | GLY72 |
| B | ASN73 |
| B | GLY74 |
| B | GLU75 |
| B | ARG113 |
| B | HOH2028 |
| B | HOH2113 |
| B | HOH2114 |
| B | HOH2115 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE R10 C 200 |
| Chain | Residue |
| C | ASP11 |
| C | HIS12 |
| C | TYR46 |
| C | GLY69 |
| C | GLY70 |
| C | SER71 |
| C | GLY72 |
| C | ASN73 |
| C | GLY74 |
| C | GLU75 |
| C | ARG113 |
| C | HOH2028 |
| C | HOH2113 |
| C | HOH2114 |
| C | HOH2115 |
| D | HIS102 |
| D | ARG137 |
| D | ARG141 |
| D | HOH2098 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 300 |
| Chain | Residue |
| B | ARG5 |
| C | HOH2116 |
| D | HIS152 |
| D | HOH2116 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE R10 D 200 |
| Chain | Residue |
| C | HIS102 |
| C | ASN103 |
| C | ARG137 |
| C | ARG141 |
| C | HOH2087 |
| D | ASP11 |
| D | HIS12 |
| D | TYR46 |
| D | GLY69 |
| D | GLY70 |
| D | SER71 |
| D | GLY72 |
| D | ASN73 |
| D | GLY74 |
| D | GLU75 |
| D | ARG113 |
| D | HOH2027 |
| D | HOH2121 |
| D | HOH2122 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE R10 E 200 |
| Chain | Residue |
| E | ASN103 |
| E | ARG113 |
| E | ARG137 |
| E | ARG141 |
| E | HOH2019 |
| E | HOH2070 |
| E | HOH2084 |
| E | HOH2085 |
| E | ASP11 |
| E | HIS12 |
| E | TYR46 |
| E | GLY69 |
| E | GLY70 |
| E | SER71 |
| E | GLY72 |
| E | ASN73 |
| E | GLY74 |
| E | GLU75 |
| E | HIS102 |
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 |
