Research workbench
Staphylococcus aureus ftsz-GDP in T and R states
Analyse Staphylococcus aureus ftsz-GDP in T and R states in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H5G
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsz
- UniProt
- Q6GHP9
- Ligands
- GDP, CA
- Pockets
- 7 · best druggability 0.67
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 | 306 | 45% helix, 24% strand | Q6GHP9 |
| B | Cell division protein ftsz | protein | 306 | 45% helix, 25% strand | Q6GHP9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 726 | 0.67 | 0.75 | 54 | empty |
| 2 | 222 | 0.60 | 0.81 | 40 | GDP |
| 3 | 230 | 0.53 | 0.77 | 33 | empty |
| 4 | 195 | 0.51 | 0.78 | 40 | GDP |
| 5 | 117 | 0.47 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 9 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 Q6GHP9
- Elsewhere: RCSB PDB 5H5G · PDBe 5H5G · UniProt Q6GHP9
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