Research workbench
S. aureus ftsz 12-316 F138A GDP closed form (3FCM)
Analyse S. aureus ftsz 12-316 F138A GDP closed form (3FCM) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MN6
- Type
- protein
- Length
- 599 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- P0A031
- Ligands
- GDP
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 296 | 45% helix, 24% strand | P0A031 |
| B | Cell division protein ftsz | protein | 303 | 45% helix, 23% strand | P0A031 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1070 | 0.74 | 0.77 | 84 | empty |
| 2 | 250 | 0.54 | 0.77 | 38 | GDP |
| 3 | 203 | 0.53 | 0.78 | 38 | GDP |
| 4 | 138 | 0.53 | 0.81 | 28 | empty |
| 5 | 61 | 0.36 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 254 Ų buried · 1 hydrogen bond · 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 P0A031
- Elsewhere: RCSB PDB 5MN6 · PDBe 5MN6 · UniProt P0A031
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