Research workbench
Crystal structure of NFS2, the plastidial cysteine desulfurase from arabidopsis thaliana
Analyse Crystal structure of NFS2, the plastidial cysteine desulfurase from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q75
- Type
- protein
- Length
- 826 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase 2, chloroplastic
- EC
- 2.8.1.7, 4.4.1.16
- UniProt
- Q93WX6
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cysteine desulfurase 2, chloroplastic (EC 2.8.1.7, 4.4.1.16) | protein | 413 | 44% helix, 18% strand | Q93WX6 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.72 | 0.97 | 19 | empty |
| 2 | 158 | 0.65 | 0.86 | 31 | empty |
| 3 | 93 | 0.56 | 0.86 | 23 | empty |
| 4 | 115 | 0.54 | 0.83 | 29 | empty |
| 5 | 62 | 0.30 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3895 Ų buried · 75 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor, oxidation).
Compared structures
- 4Q75 · Crystal structure of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q93WX6 · AlphaFold monomer V2.0 prediction for cysteine desulfurase 1, chloroplastic (Q93WX6) · 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 Q93WX6
- Elsewhere: RCSB PDB 4Q75 · PDBe 4Q75 · UniProt Q93WX6
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