Research workbench
X-ray structure of the D199K mutant of the cysteine desulfurase iscs from a. fulgidus
Analyse X-ray structure of the D199K mutant of the cysteine desulfurase iscs from a.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R5F
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase iscs 2
- EC
- 2.8.1.7
- UniProt
- O29689
- Ligands
- PMP, CA, CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase iscs 2 (EC 2.8.1.7) | protein | 369 | 44% helix, 17% strand | O29689 |
Ligands and binding sites
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- PG4 · Tetraethylene glycol · additive · 9 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.53 | 0.78 | 34 | CA, PMP |
Compared structures
- 4R5F · X-ray structure of the D199K mutant of the cysteine desulfurase IscS from A. fulgidus · the same entry in another collection · chain A against A, TM-score 1.00
- O29689 · AlphaFold monomer V2.0 prediction for cysteine desulfurase iscs 2 (O29689) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 O29689
- Elsewhere: RCSB PDB 4R5F · PDBe 4R5F · UniProt O29689
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