MolNFT v1 · #155927 · protein
Crystal structure of ido from bacillus thuringiensis
6LNH · L-isoleucine-4-hydroxylase: “Crystal structure of ido from bacillus thuringiensis”. X-ray diffraction, 2 ligands (HG, FE), 14 pockets (best druggability 0.78). MolNFT v1 #155927 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6LNH
- Type
- protein
- Length
- 887 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-isoleucine-4-hydroxylase
- EC
- 1.14.11.45
- UniProt
- E2GIN1
- Ligands
- HG, FE
- Pockets
- 14 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-isoleucine-4-hydroxylase (EC 1.14.11.45) | protein | 225 | 21% helix, 32% strand | E2GIN1 |
| B | L-isoleucine-4-hydroxylase (EC 1.14.11.45) | protein | 223 | 22% helix, 33% strand | E2GIN1 |
| C | L-isoleucine-4-hydroxylase (EC 1.14.11.45) | protein | 228 | 21% helix, 33% strand | E2GIN1 |
| D | L-isoleucine-4-hydroxylase (EC 1.14.11.45) | protein | 211 | 22% helix, 35% strand | E2GIN1 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 7 copies · chains A, C, B, D
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.78 | 0.80 | 68 | HG |
| 2 | 141 | 0.78 | 0.95 | 32 | empty |
| 3 | 209 | 0.72 | 0.88 | 31 | FE |
| 4 | 254 | 0.72 | 0.87 | 42 | empty |
| 5 | 321 | 0.71 | 0.84 | 34 | FE |
Interfaces
4 interfaces between chains.
- C–D · 1012 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 991 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 939 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 936 Ų buried · 12 hydrogen bonds · protein-protein
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 E2GIN1
- Elsewhere: RCSB PDB 6LNH · PDBe 6LNH · UniProt E2GIN1
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