MolNFT v1 · #17781 · protein
X-ray crystal structure of E. COLI iscs
1P3W · Cysteine desulfurase: “X-ray crystal structure of E. COLI iscs”. X-ray diffraction, 1 ligand (PLP), 3 pockets (best druggability 0.76). MolNFT v1 #17781 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1P3W
- Type
- protein
- Length
- 770 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase
- EC
- 4.4.1.-
- UniProt
- P0A6B7
- Ligands
- PLP
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Cysteine desulfurase (EC 4.4.1.-) | protein | 385 | 42% helix, 15% strand | P0A6B7 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains B, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.76 | 0.84 | 79 | PLP |
| 2 | 531 | 0.76 | 0.84 | 68 | PLP |
| 3 | 123 | 0.49 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- B–A · 2415 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
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 P0A6B7
- Elsewhere: RCSB PDB 1P3W · PDBe 1P3W · UniProt P0A6B7
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