Research workbench
Crystal structure of L-cycloserine-bound form of cysteine desulfurase sufs H121A from bacillus subtilis
Analyse Crystal structure of L-cycloserine-bound form of cysteine desulfurase sufs… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CES
- Type
- protein
- Length
- 414 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
- Ligands
- 7TS
- Pockets
- 3 · best druggability 0.51
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 | 414 | 45% helix, 18% strand | O32164 |
Ligands and binding sites
- 7TS · (5-hydroxy-6-methyl-4-{[(3-oxo-2,3-dihydro-1,2-oxazol-4-yl)amino]methyl}pyridin-3-yl)methyl dihydrogen phosphate · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.51 | 0.79 | 25 | 7TS |
| 2 | 55 | 0.37 | 0.80 | 15 | empty |
| 3 | 68 | 0.36 | 0.78 | 19 | empty |
Compared structures
- 7CES · Crystal structure of L-cycloserine-bound form of cysteine desulfurase SufS H121A from… · the same entry in another collection · chain A against A, TM-score 1.00
- O32164 · AlphaFold monomer V2.0 prediction for cysteine desulfurase sufs (O32164) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 7CES · PDBe 7CES · UniProt O32164
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