Research workbench
Crystal structure of a shikimate 5-dehydrogenase from mycobacterium fortuitum determined by iodide sad phasing
Analyse Crystal structure of a shikimate 5-dehydrogenase from mycobacterium fortuitum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XIJ
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Shikimate 5-dehydrogenase
- EC
- 1.1.1.25
- UniProt
- K0V1M6
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate 5-dehydrogenase (EC 1.1.1.25) | protein | 268 | 40% helix, 21% strand | K0V1M6 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.69 | 0.82 | 41 | SO4 |
Compared structures
- 4XIJ · Crystal Structure of a Shikimate 5-dehydrogenase from Mycobacterium fortuitum Determined… · 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 K0V1M6
- Elsewhere: RCSB PDB 4XIJ · PDBe 4XIJ · UniProt K0V1M6
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