Research workbench
Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with L-tartrate (orthorhombic crystal form)
Analyse Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PMQ
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.61
- Source
- Mycobacterium tuberculosis
- Molecule
- Tat-secreted protein Rv2525c
- UniProt
- P95028
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 1.61 · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tat-secreted protein Rv2525c | protein | 204 | 35% helix, 23% strand | P95028 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.49 | 0.78 | 24 | TLA, GOL |
Compared structures
- 4PMQ · Crystal structure of the mycobacterium tuberculosis tat-secreted protein RV2525C in… · 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 P95028
- Elsewhere: RCSB PDB 4PMQ · PDBe 4PMQ · UniProt P95028
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