Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T67754 | Target Info | |||
| Target Name | Transketolase (TK) | ||||
| Synonyms | TKT1; SDDHD; HEL107; HEL-S-48 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | TKT | ||||
| Biochemical Class | Transketolase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Xylitol 5-phosphate | Ligand Info | |||
| Canonical SMILES | C(C(C(C(COP(=O)(O)O)O)O)O)O | ||||
| InChI | 1S/C5H13O8P/c6-1-3(7)5(9)4(8)2-13-14(10,11)12/h3-9H,1-2H2,(H2,10,11,12)/t3-,4+,5+/m0/s1 | ||||
| InChIKey | VJDOAZKNBQCAGE-VPENINKCSA-N | ||||
| PubChem Compound ID | 6420179 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4KXV Human transketolase in covalent complex with donor ketose D-xylulose-5-phosphate, crystal 1 | ||||||
| Method | X-ray diffraction | Resolution | 0.97 Å | Mutation | No | [1] |
| PDB Sequence |
ESYHKPDQQK
11 LQALKDTANR21 LRISSIQATT31 AAGSGHPTSC41 CSAAEIMAVL51 FFHTMRYKSQ 61 DPRNPHNDRF71 VLSKGHAAPI81 LYAVWAEAGF91 LAEAELLNLR101 KISSDLDGHP 111 VPKQAFTDVA121 TGSLGQGLGA131 ACGMAYTGKY141 FDKASYRVYC151 LLGDGELSEG 161 SVWEAMAFAS171 IYKLDNLVAI181 LDINRLGQSD191 PAPLQHQMDI201 YQKRCEAFGW 211 HAIIVDGHSV221 EELCKAFGQA231 KHQPTAIIAK241 TFKGRGITGV251 EDKESWHGKP 261 LPKNMAEQII271 QEIYSQIQSK281 KKILATPPQE291 DAPSVDIANI301 RMPSLPSYKV 311 GDKIATRKAY321 GQALAKLGHA331 SDRIIALDGD341 TKNSTFSEIF351 KKEHPDRFIE 361 CYIAEQNMVS371 IAVGCATRNR381 TVPFCSTFAA391 FFTRAFDQIR401 MAAISESNIN 411 LCGSHCGVSI421 GEDGPSQMAL431 EDLAMFRSVP441 TSTVFYPSDG451 VATEKAVELA 461 ANTKGICFIR471 TSRPENAIIY481 NNNEDFQVGQ491 AKVVLKSKDD501 QVTVIGAGVT 511 LHEALAAAEL521 LKKEKINIRV531 LDPFTIKPLD541 RKLILDSARA551 TKGRILTVED 561 HYYEGGIGEA571 VSSAVVGEPG581 ITVTHLAVNR591 VPRSGKPAEL601 LKMFGIDRDA 611 IAQAVRGLIT621
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| PDB ID: 4KXW Human transketolase in covalent complex with donor ketose D-xylulose-5-phosphate, crystal 2 | ||||||
| Method | X-ray diffraction | Resolution | 0.97 Å | Mutation | No | [1] |
| PDB Sequence |
ESYHKPDQQK
11 LQALKDTANR21 LRISSIQATT31 AAGSGHPTSC41 CSAAEIMAVL51 FFHTMRYKSQ 61 DPRNPHNDRF71 VLSKGHAAPI81 LYAVWAEAGF91 LAEAELLNLR101 KISSDLDGHP 111 VPKQAFTDVA121 TGSLGQGLGA131 ACGMAYTGKY141 FDKASYRVYC151 LLGDGELSEG 161 SVWEAMAFAS171 IYKLDNLVAI181 LDINRLGQSD191 PAPLQHQMDI201 YQKRCEAFGW 211 HAIIVDGHSV221 EELCKAFGQA231 KHQPTAIIAK241 TFKGRGITGV251 EDKESWHGKP 261 LPKNMAEQII271 QEIYSQIQSK281 KKILATPPQE291 DAPSVDIANI301 RMPSLPSYKV 311 GDKIATRKAY321 GQALAKLGHA331 SDRIIALDGD341 TKNSTFSEIF351 KKEHPDRFIE 361 CYIAEQNMVS371 IAVGCATRNR381 TVPFCSTFAA391 FFTRAFDQIR401 MAAISESNIN 411 LCGSHCGVSI421 GEDGPSQMAL431 EDLAMFRSVP441 TSTVFYPSDG451 VATEKAVELA 461 ANTKGICFIR471 TSRPENAIIY481 NNNEDFQVGQ491 AKVVLKSKDD501 QVTVIGAGVT 511 LHEALAAAEL521 LKKEKINIRV531 LDPFTIKPLD541 RKLILDSARA551 TKGRILTVED 561 HYYEGGIGEA571 VSSAVVGEPG581 ITVTHLAVNR591 VPRSGKPAEL601 LKMFGIDRDA 611 IAQAVRGLIT621 K
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Sub-?ngstr?m-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate. Nat Chem. 2013 Sep;5(9):762-7. | ||||
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