Research workbench
Crystal structure of the forkhead associated (fha) domain of the glycogen accumulation regulator (gara) from mycobacterium tuberculosis
Analyse Crystal structure of the forkhead associated (fha) domain of the glycogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RJ3
- Type
- protein
- Length
- 311 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogen accumulation regulator gara
- UniProt
- A0A2I7W7N0
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen accumulation regulator gara | protein | 105 | 0% helix, 48% strand | A0A2I7W7N0 |
| B | Glycogen accumulation regulator gara | protein | 105 | 0% helix, 46% strand | A0A2I7W7N0 |
| C | Glycogen accumulation regulator gara | protein | 101 | 0% helix, 49% strand | A0A2I7W7N0 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · 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 | 491 | 0.67 | 0.78 | 66 | empty |
| 2 | 58 | 0.32 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 558 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 533 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 128 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7RJ3 · Crystal Structure of the Forkhead Associated (FHA) Domain of the Glycogen Accumulation… · 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 A0A2I7W7N0
- Elsewhere: RCSB PDB 7RJ3 · PDBe 7RJ3 · UniProt A0A2I7W7N0
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