Research workbench
Crystal structure of iscs from mycobacterium tuberculosis
Analyse Crystal structure of iscs from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ISY
- Type
- protein
- Length
- 1,522 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase
- EC
- 2.8.1.7
- UniProt
- O53272
- Ligands
- SO4
- Pockets
- 16 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase (EC 2.8.1.7) | protein | 379 | 45% helix, 16% strand | O53272 |
| B | Cysteine desulfurase (EC 2.8.1.7) | protein | 379 | 45% helix, 16% strand | O53272 |
| C | Cysteine desulfurase (EC 2.8.1.7) | protein | 383 | 45% helix, 15% strand | O53272 |
| D | Cysteine desulfurase (EC 2.8.1.7) | protein | 381 | 46% helix, 16% strand | O53272 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 606 | 0.78 | 0.84 | 79 | empty |
| 2 | 572 | 0.75 | 0.82 | 54 | GOL |
| 3 | 106 | 0.73 | 0.94 | 28 | empty |
| 4 | 107 | 0.73 | 0.94 | 26 | empty |
| 5 | 69 | 0.72 | 0.97 | 25 | empty |
Interfaces
5 interfaces between chains.
- B–D · 2265 Ų buried · 39 hydrogen bonds · protein-protein
- A–D · 539 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 472 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 345 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 19 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor).
Compared structures
- 4ISY · Crystal structure of IscS from Mycobacterium tuberculosis · the same entry in another collection · 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 O53272
- Elsewhere: RCSB PDB 4ISY · PDBe 4ISY · UniProt O53272
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