6HA3
Human transketolase variant E160Q in covalent complex with donor ketose D-fructose-6-phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004802 | molecular_function | transketolase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005777 | cellular_component | peroxisome |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006098 | biological_process | pentose-phosphate shunt |
A | 0006796 | biological_process | phosphate-containing compound metabolic process |
A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
A | 0016604 | cellular_component | nuclear body |
A | 0016740 | molecular_function | transferase activity |
A | 0016744 | molecular_function | transketolase or transaldolase activity |
A | 0019637 | biological_process | organophosphate metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0031982 | cellular_component | vesicle |
A | 0040008 | biological_process | regulation of growth |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
A | 1901159 | biological_process | xylulose 5-phosphate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 38 |
Details | binding site for residue T6F A 701 |
Chain | Residue |
A | HIS37 |
A | ASP155 |
A | GLY156 |
A | GLU157 |
A | GLN160 |
A | ASN185 |
A | LEU187 |
A | GLN189 |
A | LYS244 |
A | HIS258 |
A | ARG318 |
A | SER40 |
A | ASP341 |
A | SER345 |
A | ILE364 |
A | GLU366 |
A | PHE389 |
A | PHE392 |
A | ARG395 |
A | HIS416 |
A | ASP424 |
A | GLN428 |
A | LYS75 |
A | ARG474 |
A | EDO702 |
A | EDO714 |
A | CA715 |
A | MG716 |
A | HOH958 |
A | HOH1060 |
A | HOH1076 |
A | HOH1102 |
A | HIS77 |
A | HIS110 |
A | GLY123 |
A | SER124 |
A | LEU125 |
A | GLY154 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue EDO A 702 |
Chain | Residue |
A | SER35 |
A | GLY36 |
A | HIS37 |
A | GLY259 |
A | ASP424 |
A | ARG474 |
A | T6F701 |
A | HOH1108 |
A | HOH1175 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 703 |
Chain | Residue |
A | PHE71 |
A | VAL72 |
A | LEU73 |
A | LEU82 |
A | PHE117 |
A | THR118 |
A | HOH867 |
A | HOH978 |
A | HOH1173 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 704 |
Chain | Residue |
A | TYR564 |
A | ALA588 |
A | ASN590 |
A | HOH871 |
A | HOH917 |
A | HOH1012 |
A | HOH1133 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 705 |
Chain | Residue |
A | ARG21 |
A | ALA84 |
A | GLU88 |
A | GLU94 |
A | LEU97 |
A | LYS283 |
A | HOH807 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 706 |
Chain | Residue |
A | PRO63 |
A | ASN68 |
A | ASP69 |
A | ARG70 |
A | PHE71 |
A | ARG379 |
A | HOH864 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 707 |
Chain | Residue |
A | LEU92 |
A | ASP106 |
A | LEU107 |
A | GLN115 |
A | HOH835 |
A | HOH875 |
A | HOH972 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue NA A 708 |
Chain | Residue |
A | ASN411 |
A | ALA461 |
A | THR464 |
A | CYS468 |
A | HOH897 |
A | HOH1165 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 709 |
Chain | Residue |
A | GLN10 |
A | ASN590 |
A | ARG591 |
A | HOH891 |
A | HOH1337 |
A | HOH1357 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO A 710 |
Chain | Residue |
A | ASP62 |
A | ASN65 |
A | PRO66 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 711 |
Chain | Residue |
A | PRO475 |
A | ASN477 |
A | VAL510 |
A | PRO598 |
A | HOH882 |
A | HOH910 |
A | HOH1325 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 712 |
Chain | Residue |
A | ASP155 |
A | GLY156 |
A | SER159 |
A | PRO194 |
A | LEU195 |
A | TYR202 |
A | EDO713 |
A | HOH974 |
A | HOH982 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue EDO A 713 |
Chain | Residue |
A | LEU158 |
A | LEU195 |
A | ARG205 |
A | PHE209 |
A | EDO712 |
A | HOH842 |
A | HOH970 |
A | HOH982 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue EDO A 714 |
Chain | Residue |
A | LYS260 |
A | ARG318 |
A | ASN344 |
A | ARG474 |
A | T6F701 |
A | HOH1060 |
A | HOH1284 |
A | HOH1289 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue CA A 715 |
Chain | Residue |
A | ASP155 |
A | ASN185 |
A | LEU187 |
A | T6F701 |
A | HOH958 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue MG A 716 |
Chain | Residue |
A | ASP155 |
A | ASN185 |
A | LEU187 |
A | T6F701 |
A | HOH958 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU366 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS37 | |
A | ARG318 | |
A | SER345 | |
A | HIS416 | |
A | ASP424 | |
A | ARG474 |
site_id | SWS_FT_FI3 |
Number of Residues | 11 |
Details | BINDING: |
Chain | Residue | Details |
A | SER40 | |
A | PHE392 | |
A | GLN428 | |
A | HIS77 | |
A | GLY123 | |
A | ASP155 | |
A | GLY156 | |
A | ASN185 | |
A | LEU187 | |
A | LYS244 | |
A | HIS258 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000250 |
Chain | Residue | Details |
A | HIS37 | |
A | HIS258 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER3 | |
A | SER104 |
site_id | SWS_FT_FI7 |
Number of Residues | 7 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS6 | |
A | LYS11 | |
A | LYS144 | |
A | LYS204 | |
A | LYS241 | |
A | LYS260 | |
A | LYS603 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P40142 |
Chain | Residue | Details |
A | LYS232 | |
A | LYS538 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | TYR275 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR287 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER295 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50137 |
Chain | Residue | Details |
A | SER345 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS352 |