1LK7
Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid
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 |
| A | 0044281 | biological_process | small molecule metabolic process |
| 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 |
| B | 0044281 | biological_process | small molecule metabolic process |
| 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 |
| C | 0044281 | biological_process | small molecule metabolic process |
| 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 |
| D | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 2001 |
| Chain | Residue |
| A | GLY99 |
| A | GLY101 |
| A | ALA102 |
| A | ALA103 |
| A | GLU107 |
| A | DER1001 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 2002 |
| Chain | Residue |
| B | ALA103 |
| B | GLU107 |
| B | DER1002 |
| B | GLY99 |
| B | GLY101 |
| B | ALA102 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL C 2003 |
| Chain | Residue |
| C | GLY99 |
| C | GLY101 |
| C | ALA102 |
| C | ALA103 |
| C | GLU107 |
| C | DER1003 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL D 2004 |
| Chain | Residue |
| D | GLY99 |
| D | GLY101 |
| D | ALA102 |
| D | ALA103 |
| D | GLU107 |
| D | DER1004 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 2005 |
| Chain | Residue |
| A | SER57 |
| A | TYR58 |
| A | GLN59 |
| A | ASP174 |
| C | LYS167 |
| C | ASP168 |
| C | GLY169 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CL B 2006 |
| Chain | Residue |
| B | SER57 |
| B | TYR58 |
| B | GLN59 |
| B | ASP174 |
| B | HOH2036 |
| D | LYS167 |
| D | ASP168 |
| D | GLY169 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL C 2007 |
| Chain | Residue |
| A | LYS167 |
| A | ASP168 |
| A | GLY169 |
| C | SER57 |
| C | TYR58 |
| C | GLN59 |
| C | ASP174 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL D 2008 |
| Chain | Residue |
| B | LYS167 |
| B | ASP168 |
| D | SER57 |
| D | TYR58 |
| D | GLN59 |
| D | ASP174 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 2009 |
| Chain | Residue |
| A | VAL165 |
| A | ASN166 |
| C | VAL165 |
| C | ASN166 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 2010 |
| Chain | Residue |
| B | VAL165 |
| B | ASN166 |
| D | VAL165 |
| D | ASN166 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 2011 |
| Chain | Residue |
| A | ASN175 |
| A | HOH2019 |
| A | HOH2049 |
| A | HOH2050 |
| B | ASN175 |
| B | HOH2026 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 2012 |
| Chain | Residue |
| C | ASN175 |
| C | HOH2051 |
| C | HOH2052 |
| D | ASN175 |
| D | HOH2039 |
| D | HOH2040 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DER A 1001 |
| Chain | Residue |
| A | THR28 |
| A | SER30 |
| A | THR31 |
| A | ASP85 |
| A | GLY86 |
| A | ALA87 |
| A | ASP88 |
| A | LYS98 |
| A | GLY99 |
| A | ARG100 |
| A | GLY101 |
| A | GLU107 |
| A | LYS125 |
| A | CL2001 |
| A | HOH2052 |
| A | HOH2053 |
| A | HOH2098 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DER B 1002 |
| Chain | Residue |
| B | GLU107 |
| B | LYS125 |
| B | CL2002 |
| B | HOH2031 |
| B | HOH2038 |
| D | HOH2082 |
| B | THR28 |
| B | SER30 |
| B | THR31 |
| B | ASP85 |
| B | GLY86 |
| B | ALA87 |
| B | ASP88 |
| B | LYS98 |
| B | GLY99 |
| B | GLY101 |
| site_id | BC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE DER C 1003 |
| Chain | Residue |
| C | THR28 |
| C | GLY29 |
| C | SER30 |
| C | THR31 |
| C | ASP85 |
| C | GLY86 |
| C | ALA87 |
| C | ASP88 |
| C | LYS98 |
| C | GLY99 |
| C | ARG100 |
| C | GLY101 |
| C | GLU107 |
| C | LYS125 |
| C | CL2003 |
| C | HOH2020 |
| C | HOH2055 |
| C | HOH2059 |
| C | HOH2074 |
| C | HOH2100 |
| site_id | BC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DER D 1004 |
| Chain | Residue |
| D | THR28 |
| D | SER30 |
| D | THR31 |
| D | ASP85 |
| D | GLY86 |
| D | ALA87 |
| D | ASP88 |
| D | LYS98 |
| D | GLY99 |
| D | GLY101 |
| D | GLU107 |
| D | LYS125 |
| D | CL2004 |
| D | HOH2035 |
| D | HOH2054 |
| D | HOH2055 |
| D | HOH2105 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:12057201 |
| Chain | Residue | Details |
| A | GLU107 | |
| B | GLU107 | |
| C | GLU107 | |
| D | GLU107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12057201, ECO:0007744|PDB:1LK7 |
| Chain | Residue | Details |
| A | THR28 | |
| D | THR28 | |
| D | ASP85 | |
| D | LYS98 | |
| A | ASP85 | |
| A | LYS98 | |
| B | THR28 | |
| B | ASP85 | |
| B | LYS98 | |
| C | THR28 | |
| C | ASP85 | |
| C | LYS98 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12057201, ECO:0007744|PDB:1LK7 |
| Chain | Residue | Details |
| A | LYS125 | |
| B | LYS125 | |
| C | LYS125 | |
| D | LYS125 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Plays a direct or indirect catalytic role |
| Chain | Residue | Details |
| A | ASP85 | |
| B | ASP85 | |
| C | ASP85 | |
| D | ASP85 |
