MolNFT v1 · #120596 · protein
Staphylococcus aureus ftsz-GDP R29A mutant in T state
5H5H · Cell division protein ftsz: “Staphylococcus aureus ftsz-GDP R29A mutant in T state”. X-ray diffraction, 2 ligands (GDP, CA), 3 pockets (best druggability 0.58). MolNFT v1 #120596 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5H5H
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- Q6GHP9
- Ligands
- GDP, CA
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsz | protein | 305 | 46% helix, 24% strand | Q6GHP9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.58 | 0.79 | 44 | GDP |
| 2 | 139 | 0.54 | 0.81 | 23 | empty |
| 3 | 85 | 0.42 | 0.79 | 19 | 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 Q6GHP9
- Elsewhere: RCSB PDB 5H5H · PDBe 5H5H · UniProt Q6GHP9
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