Research workbench
Structure of cite complexed with triphosphate group of ATP form mycobacterium tuberculosis
Analyse Structure of cite complexed with triphosphate group of ATP form mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U5V
- 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
- Ligands
- ATP
- 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
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 | 149 | 0.51 | 0.79 | 28 | empty |
| 2 | 52 | 0.29 | 0.76 | 13 | empty |
Compared structures
- 1U5V · Structure of CitE complexed with triphosphate group of ATP form 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 1U5V · PDBe 1U5V · UniProt O06162
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