Research workbench
Crystal structure of the protein L1841, unknown member of enolase superfamily from bradyrhizobium japonicum
Analyse Crystal structure of the protein L1841, unknown member of enolase superfamily… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TZZ
- Type
- protein
- Length
- 753 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein L1841
- UniProt
- Q89FH0
- Ligands
- MG
- Pockets
- 7 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein L1841 | protein | 374 | 39% helix, 18% strand | Q89FH0 |
| B | Hypothetical protein L1841 | protein | 379 | 40% helix, 18% strand | Q89FH0 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.62 | 0.83 | 36 | empty |
| 2 | 138 | 0.50 | 0.79 | 25 | empty |
| 3 | 123 | 0.47 | 0.78 | 24 | empty |
| 4 | 89 | 0.43 | 0.79 | 14 | empty |
| 5 | 108 | 0.42 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 394 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1TZZ · Crystal structure of the protein L1841, unknown member of enolase superfamily from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q89FH0 · AlphaFold monomer V2.0 prediction for D(-)-tartrate dehydratase (Q89FH0) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q89FH0
- Elsewhere: RCSB PDB 1TZZ · PDBe 1TZZ · UniProt Q89FH0
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