3OVP
Crystal Structure of hRPE
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 FE2 A 229 |
Chain | Residue |
A | HIS35 |
A | ASP37 |
A | HIS70 |
A | ASP175 |
A | HOH258 |
A | HOH266 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE XPE A 230 |
Chain | Residue |
A | ASP171 |
A | MET193 |
A | GLY4 |
A | LYS6 |
A | ASP32 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE XPE A 231 |
Chain | Residue |
A | PRO121 |
A | MET153 |
A | HOH325 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE XPE A 232 |
Chain | Residue |
A | HIS184 |
A | LYS185 |
A | HOH238 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B 229 |
Chain | Residue |
B | HIS35 |
B | ASP37 |
B | HIS70 |
B | ASP175 |
B | HOH256 |
B | HOH261 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE XPE B 230 |
Chain | Residue |
B | GLY4 |
B | LYS6 |
B | ASP32 |
B | PHE66 |
B | ASP171 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE XPE B 231 |
Chain | Residue |
B | GLN63 |
B | GLY87 |
B | ALA88 |
B | GLY112 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XPE B 232 |
Chain | Residue |
B | GLU126 |
B | TRP162 |
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 | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR |
Chain | Residue | Details |
A | ASP37 | |
B | ASP37 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR |
Chain | Residue | Details |
A | ASP175 | |
B | ASP175 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVR |
Chain | Residue | Details |
A | SER10 | |
B | SER10 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9, ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3 |
Chain | Residue | Details |
A | HIS35 | |
A | ASP37 | |
A | ASP175 | |
B | HIS35 | |
B | ASP37 | |
B | ASP175 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR |
Chain | Residue | Details |
A | HIS70 | |
A | GLY146 | |
A | GLY197 | |
B | HIS70 | |
B | GLY146 | |
B | GLY197 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |