Research workbench
Structure of citrate lyase beta subunit from mycobacterium tuberculosis
Analyse Structure of citrate lyase beta subunit from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U5H
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cite
- EC
- 4.1.3.6
- UniProt
- O06162
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cite (EC 4.1.3.6) | protein | 223 | 44% helix, 18% strand | O06162 |
Ligands and binding sites
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.51 | 0.79 | 23 | empty |
| 2 | 61 | 0.29 | 0.75 | 16 | empty |
Compared structures
- 1U5H · Structure of Citrate Lyase beta subunit from Mycobacterium tuberculosis · 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 O06162
- Elsewhere: RCSB PDB 1U5H · PDBe 1U5H · UniProt O06162
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