Research workbench
Ftsz dimer, mggtp soak (M. jannaschii)
Analyse Ftsz dimer, mggtp soak (M. jannaschii) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W5A
- Type
- protein
- Length
- 668 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz homolog 1
- UniProt
- Q57816
- Ligands
- GTP, MG
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz homolog 1 | protein | 333 | 47% helix, 24% strand | Q57816 |
| B | Cell division protein ftsz homolog 1 | protein | 335 | 47% helix, 24% strand | Q57816 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1050 | 0.81 | 0.82 | 74 | GTP, MG |
| 2 | 249 | 0.62 | 0.81 | 30 | empty |
| 3 | 175 | 0.48 | 0.77 | 32 | GTP |
| 4 | 94 | 0.46 | 0.80 | 23 | empty |
| 5 | 65 | 0.43 | 0.82 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1129 Ų buried · 17 hydrogen bonds · protein-protein
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 1W5A · PDBe 1W5A · UniProt Q57816
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