Research workbench
Ftsz GDP M. jannaschii
Analyse Ftsz GDP M. jannaschii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VAP
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz homolog 1
- UniProt
- Q57816
- Ligands
- GDP
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz homolog 1 | protein | 335 | 45% helix, 25% strand | Q57816 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.50 | 0.77 | 31 | GDP |
| 2 | 70 | 0.43 | 0.81 | 17 | empty |
| 3 | 93 | 0.36 | 0.75 | 16 | empty |
Compared structures
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 Q57816
- Elsewhere: RCSB PDB 2VAP · PDBe 2VAP · UniProt Q57816
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