MolNFT v1 · #139894 · protein
Crystal structure of transketolase in complex with aminopyrimidine and cysteine sulfonic acid adduct from pichia stipitis
5XTL: “Crystal structure of transketolase in complex with aminopyrimidine and cysteine sulfonic acid adduct from…”. X-ray diffraction, 3 ligands (P23, 8GF, CA), 5 pockets (best druggability 0.60). MolNFT v1 #139894 on GenesisL1: 3D…
- PDB
- 5XTL
- Type
- protein
- Length
- 675 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transketolase
- EC
- 2.2.1.1
- UniProt
- P34736
- Ligands
- P23, 8GF, CA
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transketolase (EC 2.2.1.1) | protein | 675 | 45% helix, 13% strand | P34736 |
Ligands and binding sites
- P23 · Propyl trihydrogen diphosphate · ligand · chains A
- 8GF · 2-methylpyrimidin-4-amine · ligand · chains A
- CA · Calcium ion · metal · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.60 | 0.79 | 46 | PEG |
| 2 | 79 | 0.54 | 0.86 | 16 | P23, CA |
| 3 | 96 | 0.38 | 0.76 | 17 | empty |
| 4 | 74 | 0.30 | 0.73 | 15 | empty |
| 5 | 50 | 0.29 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, oxidation).
Compared structures
- 5XTL · Crystal Structure of Transketolase in complex with aminopyrimidine and cysteine sulfonic… · the same entry in another collection · chain A against A, TM-score 1.00
- P34736 · AlphaFold monomer V2.0 prediction for transketolase (P34736) · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P34736
- Elsewhere: RCSB PDB 5XTL · PDBe 5XTL · UniProt P34736
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