Research workbench
Crystal structure of M. tuberculosis pknb LEU33ASP/VAL222ASP double mutant in complex with ADP
Analyse Crystal structure of M. tuberculosis pknb LEU33ASP/VAL222ASP double mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F61
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase pknb
- EC
- 2.7.11.1
- UniProt
- P0A5S4
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pknb (EC 2.7.11.1) | protein | 271 | 39% helix, 21% strand | P0A5S4 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.71 | 0.81 | 49 | ADP, MG |
Compared structures
- 3F61 · Crystal Structure of M. tuberculosis PknB Leu33Asp/Val222Asp double mutant in complex… · 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 P0A5S4
- Elsewhere: RCSB PDB 3F61 · PDBe 3F61 · UniProt P0A5S4
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