3OVR
Crystal Structure of hRPE and D-Xylulose 5-Phosphate Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 229 |
| Chain | Residue |
| A | HIS35 |
| A | ASP37 |
| A | HIS70 |
| A | ASP175 |
| A | 5SP230 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 5SP A 230 |
| Chain | Residue |
| A | MET39 |
| A | HIS70 |
| A | MET72 |
| A | PRO145 |
| A | GLY146 |
| A | PHE147 |
| A | GLY149 |
| A | ASP175 |
| A | GLY176 |
| A | GLY177 |
| A | GLY197 |
| A | SER198 |
| A | FE2229 |
| A | HOH245 |
| A | HOH247 |
| A | HOH258 |
| A | HOH271 |
| A | HOH283 |
| A | SER10 |
| A | LEU12 |
| A | HIS35 |
| A | ASP37 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE XPE A 231 |
| Chain | Residue |
| A | TRP131 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE XPE A 232 |
| Chain | Residue |
| A | GLY4 |
| A | LYS6 |
| A | ASP32 |
| A | ASP171 |
| A | MET193 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE XPE A 233 |
| Chain | Residue |
| A | ARG58 |
| A | GLN63 |
| A | PHE66 |
| A | GLY87 |
| A | ALA88 |
| A | ASN89 |
| A | GLY112 |
| A | LYS114 |
| A | HOH343 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE XPE A 234 |
| Chain | Residue |
| A | PRO158 |
| A | HIS161 |
| A | TRP162 |
| A | GLN166 |
| A | GLU188 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 229 |
| Chain | Residue |
| B | HIS35 |
| B | ASP37 |
| B | HIS70 |
| B | ASP175 |
| B | 5SP230 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE 5SP B 230 |
| Chain | Residue |
| B | SER10 |
| B | LEU12 |
| B | HIS35 |
| B | ASP37 |
| B | MET39 |
| B | HIS70 |
| B | MET72 |
| B | PRO145 |
| B | GLY146 |
| B | PHE147 |
| B | GLY148 |
| B | GLY149 |
| B | ASP175 |
| B | GLY176 |
| B | GLY177 |
| B | GLY197 |
| B | SER198 |
| B | FE2229 |
| B | HOH242 |
| B | HOH246 |
| B | HOH263 |
| B | HOH319 |
| B | HOH321 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE XPE B 231 |
| Chain | Residue |
| B | GLY4 |
| B | LYS6 |
| B | ASP32 |
| B | ASP171 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE XPE B 232 |
| Chain | Residue |
| B | GLY122 |
| B | THR123 |
| B | TYR127 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE XPE B 233 |
| Chain | Residue |
| B | ALA88 |
| B | ASN89 |
| B | GLY112 |
Functional Information from PROSITE/UniProt
| site_id | PS01085 |
| Number of Residues | 15 |
| Details | RIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. LHLDVmDghFVpNiT |
| Chain | Residue | Details |
| A | LEU34-THR48 |
| site_id | PS01086 |
| Number of Residues | 23 |
| Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. AlVMTVePgfgGQkFmedmmpKV |
| Chain | Residue | Details |
| A | ALA138-VAL160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699) from Homo sapiens at 2.20 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"3OVP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QC3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
