Research workbench
Nifs from helicobacter pylori
Analyse Nifs from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WT2
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase iscs
- EC
- 2.8.1.7
- UniProt
- O25008
- Ligands
- PLP, CL
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase iscs (EC 2.8.1.7) | protein | 355 | 40% helix, 17% strand | O25008 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- CL · Chloride ion · ion · chains A
- IPA · Isopropyl alcohol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.34 | 0.77 | 19 | empty |
| 2 | 66 | 0.29 | 0.73 | 17 | IPA |
Modifications
Observed in the structure: 1 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 O25008
- Elsewhere: RCSB PDB 5WT2 · PDBe 5WT2 · UniProt O25008
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