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Crystal structure of bi-functional enzyme
Analyse Crystal structure of bi-functional enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J2L
- 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
- Ligands
- ZN, MG
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 45% 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 | 44% helix, 20% strand | P37793 |
| B | Histidine biosynthesis bifunctional protein hisie (EC 3.5.4.19, 3.6.1.31) | protein | 185 | 46% helix, 21% strand | P37793 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 419 | 0.61 | 0.76 | 39 | ZN |
| 2 | 92 | 0.48 | 0.81 | 19 | ZN |
| 3 | 68 | 0.37 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 3405 Ų buried · 37 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 6J2L · PDBe 6J2L · UniProt P37793
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