MolNFT v1 · #153062 · protein
Crystal structure of bi-functional enzyme
6J22 · Histidine biosynthesis bifunctional protein hisie: “Crystal structure of bi-functional enzyme”. X-ray diffraction, 3 pockets (best druggability 0.64). MolNFT v1 #153062 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6J22
- Type
- protein
- Length
- 385 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine biosynthesis bifunctional protein hisie
- EC
- 3.5.4.19, 3.6.1.31
- UniProt
- P37793
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine biosynthesis bifunctional protein hisie (EC 3.5.4.19, 3.6.1.31) | protein | 200 | 43% helix, 20% strand | P37793 |
| B | Histidine biosynthesis bifunctional protein hisie (EC 3.5.4.19, 3.6.1.31) | protein | 185 | 43% helix, 21% strand | P37793 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.64 | 0.76 | 45 | empty |
| 2 | 182 | 0.49 | 0.77 | 35 | empty |
| 3 | 77 | 0.35 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3377 Ų buried · 33 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 P37793
- Elsewhere: RCSB PDB 6J22 · PDBe 6J22 · UniProt P37793
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.