MolNFT v1 · #142069 · protein
Sufs from bacillus subtilis in the resting state
5ZS9 · Cysteine desulfurase sufs: “Sufs from bacillus subtilis in the resting state”. X-ray diffraction, 2 pockets (best druggability 0.40). MolNFT v1 #142069 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ZS9
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase sufs
- EC
- 2.8.1.7
- UniProt
- O32164
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase sufs (EC 2.8.1.7) | protein | 405 | 45% helix, 18% strand | O32164 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.40 | 0.78 | 18 | empty |
| 2 | 58 | 0.36 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 1 modified (cofactor).
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 O32164
- Elsewhere: RCSB PDB 5ZS9 · PDBe 5ZS9 · UniProt O32164
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