3QC3
Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699) from HOMO SAPIENS at 2.20 A resolution
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 | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 229 |
| Chain | Residue |
| A | HIS35 |
| A | ASP37 |
| A | HIS70 |
| A | ASP175 |
| A | GOL232 |
| A | HOH463 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 230 |
| Chain | Residue |
| A | ASP175 |
| A | GOL232 |
| A | HOH463 |
| A | HIS35 |
| A | ASP37 |
| A | HIS70 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 231 |
| Chain | Residue |
| A | HIS35 |
| A | ASP37 |
| A | HIS70 |
| A | ASP175 |
| A | GOL232 |
| A | HOH463 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 232 |
| Chain | Residue |
| A | ASP37 |
| A | MSE39 |
| A | HIS70 |
| A | MSE72 |
| A | PRO145 |
| A | GLY146 |
| A | ASP175 |
| A | ZN229 |
| A | NI230 |
| A | FE231 |
| A | HOH463 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 229 |
| Chain | Residue |
| B | HIS35 |
| B | ASP37 |
| B | HIS70 |
| B | ASP175 |
| B | GOL232 |
| B | HOH456 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 230 |
| Chain | Residue |
| B | HIS35 |
| B | ASP37 |
| B | HIS70 |
| B | ASP175 |
| B | GOL232 |
| B | HOH456 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 231 |
| Chain | Residue |
| B | HIS35 |
| B | ASP37 |
| B | HIS70 |
| B | ASP175 |
| B | GOL232 |
| B | HOH456 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL B 232 |
| Chain | Residue |
| B | ASP37 |
| B | MSE39 |
| B | HIS70 |
| B | MSE72 |
| B | PRO145 |
| B | GLY146 |
| B | ASP175 |
| B | ZN229 |
| B | NI230 |
| B | FE231 |
| B | HOH404 |
| B | HOH456 |
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 | Binding site: {"evidences":[{"source":"PubMed","id":"20923965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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_FI4 |
| Number of Residues | 8 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
