1LK5
Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006014 | biological_process | D-ribose 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 |
| B | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006014 | biological_process | D-ribose 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 |
| C | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006014 | biological_process | D-ribose 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 |
| D | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006014 | biological_process | D-ribose 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1001 |
| Chain | Residue |
| A | GLY99 |
| A | GLY101 |
| A | ALA102 |
| A | ALA103 |
| A | GLU107 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 1002 |
| Chain | Residue |
| B | GLU107 |
| B | HOH1017 |
| B | GLY99 |
| B | GLY101 |
| B | ALA102 |
| B | ALA103 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 1003 |
| Chain | Residue |
| C | GLY99 |
| C | GLY101 |
| C | ALA102 |
| C | ALA103 |
| C | GLU107 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL D 1004 |
| Chain | Residue |
| D | GLY99 |
| D | GLY101 |
| D | ALA102 |
| D | ALA103 |
| D | GLU107 |
| D | HOH1020 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 1005 |
| Chain | Residue |
| A | SER57 |
| A | TYR58 |
| A | GLN59 |
| A | ASP174 |
| C | LYS167 |
| C | ASP168 |
| C | GLY169 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 1006 |
| Chain | Residue |
| B | TYR58 |
| B | GLN59 |
| B | ASP174 |
| D | LYS167 |
| D | ASP168 |
| D | GLY169 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL C 1007 |
| Chain | Residue |
| A | LYS167 |
| A | ASP168 |
| A | GLY169 |
| C | SER57 |
| C | TYR58 |
| C | GLN59 |
| C | ASP174 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL D 1008 |
| Chain | Residue |
| B | LYS167 |
| B | ASP168 |
| B | GLY169 |
| D | SER57 |
| D | TYR58 |
| D | GLN59 |
| D | ASP174 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1009 |
| Chain | Residue |
| A | VAL165 |
| A | ASN166 |
| C | VAL165 |
| C | ASN166 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1010 |
| Chain | Residue |
| B | VAL165 |
| B | ASN166 |
| D | VAL165 |
| D | ASN166 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1011 |
| Chain | Residue |
| A | ASN175 |
| A | HOH1016 |
| A | HOH1024 |
| B | ASN175 |
| B | HOH1016 |
| B | HOH1026 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 1012 |
| Chain | Residue |
| C | ASN175 |
| C | HOH1039 |
| C | HOH1047 |
| D | ASN175 |
| D | HOH1014 |
| D | HOH1069 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12057201","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057201","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Plays a direct or indirect catalytic role"} |
| Chain | Residue | Details |
