Research workbench
Shikimate kinase from mycobacterium tuberculosis in complex with ADP, open lid (conf. a)
Analyse Shikimate kinase from mycobacterium tuberculosis in complex with ADP, open lid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IYU
- Type
- protein
- Length
- 167 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, CL
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate kinase (EC 2.7.1.71) | protein | 167 | 57% helix, 12% strand | P0A4Z2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2IYU · Shikimate kinase from Mycobacterium tuberculosis in complex with ADP, open LID (conf. A) · 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 2IYU · PDBe 2IYU · UniProt P0A4Z2
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