6HAD
Human transketolase variant E160Q
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 | 6 |
Details | binding site for residue NA A 701 |
Chain | Residue |
A | ASN411 |
A | ALA461 |
A | THR464 |
A | CYS468 |
A | HOH866 |
A | HOH1230 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA A 702 |
Chain | Residue |
A | TPP704 |
A | HOH926 |
A | ASP155 |
A | ASN185 |
A | LEU187 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG A 703 |
Chain | Residue |
A | ASP155 |
A | ASN185 |
A | LEU187 |
A | TPP704 |
A | HOH926 |
site_id | AC4 |
Number of Residues | 25 |
Details | binding site for residue TPP A 704 |
Chain | Residue |
A | SER40 |
A | LYS75 |
A | HIS77 |
A | GLY123 |
A | SER124 |
A | LEU125 |
A | GLY154 |
A | ASP155 |
A | GLY156 |
A | GLU157 |
A | GLN160 |
A | ASN185 |
A | LEU187 |
A | GLN189 |
A | LYS244 |
A | HIS258 |
A | ASP341 |
A | ILE364 |
A | GLU366 |
A | PHE392 |
A | ARG395 |
A | GLN428 |
A | CA702 |
A | MG703 |
A | HOH926 |
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 |