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Crystal structure of shikimate kinase from mycobacterium tuberculosis in complex with mgadp and PT(II) at 1.8 ångström resolution
Analyse Crystal structure of shikimate kinase from mycobacterium tuberculosis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L4U
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Shikimate kinase
- EC
- 2.7.1.71
- UniProt
- P0A4Z2
- Ligands
- ADP, PT, MG, CL
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate kinase (EC 2.7.1.71) | protein | 165 | 58% helix, 12% strand | P0A4Z2 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- PT · Platinum (II) ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 6 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
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 | 268 | 0.61 | 0.80 | 35 | MG, CL, ADP |
Compared structures
- 1L4U · Crystal structure of shikimate kinase from mycobacterium tuberculosis in complex with… · 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 P0A4Z2
- Elsewhere: RCSB PDB 1L4U · PDBe 1L4U · UniProt P0A4Z2
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