Research workbench
Crystal structure of thiamine-monophosphate kinase from stenotrophomonas maltophilia K279A
Analyse Crystal structure of thiamine-monophosphate kinase from stenotrophomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XEP
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thiamine-monophosphate kinase
- EC
- 2.7.4.16
- UniProt
- B2FNL5
- Ligands
- NA
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine-monophosphate kinase (EC 2.7.4.16) | protein | 316 | 37% helix, 25% strand | B2FNL5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.39 | 0.79 | 26 | empty |
Compared structures
- 6XEP · Crystal structure of Thiamine-monophosphate kinase from Stenotrophomonas maltophilia K279a · the same entry in another collection · 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 B2FNL5
- Elsewhere: RCSB PDB 6XEP · PDBe 6XEP · UniProt B2FNL5
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