Research workbench
Crystal structure of E.COLI iscs-tusa complex (form 1)
Analyse Crystal structure of E.COLI iscs-tusa complex (form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LVJ
- Type
- protein
- Length
- 926 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase; Sulfurtransferase tusa
- EC
- 2.8.1.7, 2.8.1.-
- UniProt
- P0A6B9, P0A892
- Ligands
- PLP
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase (EC 2.8.1.7) | protein | 384 | 41% helix, 16% strand | P0A6B9 |
| B | Cysteine desulfurase (EC 2.8.1.7) | protein | 388 | 40% helix, 16% strand | P0A6B9 |
| C, D | Sulfurtransferase tusa (EC 2.8.1.-) | protein | 77 | 29% helix, 29% strand | P0A892 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.81 | 0.82 | 94 | PLP |
| 2 | 1065 | 0.78 | 0.80 | 98 | PLP |
| 3 | 123 | 0.50 | 0.80 | 22 | empty |
| 4 | 82 | 0.42 | 0.79 | 17 | empty |
| 5 | 69 | 0.38 | 0.79 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2285 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 774 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 716 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 109 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 41 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 3LVJ · Crystal Structure of E.coli IscS-TusA complex (form 1) · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6B9 · AlphaFold monomer V2.0 prediction for cysteine desulfurase iscs (P0A6B9) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P0A892 · AlphaFold monomer V2.0 prediction for sulfur carrier protein tusa (P0A892) · a predicted model of the same protein · chain C 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 P0A6B9
- Every structure of UniProt P0A892
- Elsewhere: RCSB PDB 3LVJ · PDBe 3LVJ · UniProt P0A6B9 · UniProt P0A892
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