MolNFT v1 · #37281 · protein
Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) H89N from the acidophilic bacterium acetobacter aceti, at pH 7
2FWA: “Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) H89N from the acidophilic bacterium…”. X-ray diffraction, 2 pockets (best druggability 0.31). MolNFT v1 #37281 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2FWA
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N5-carboxyaminoimidazole ribonucleotide mutase
- UniProt
- Q2QJL3
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N5-carboxyaminoimidazole ribonucleotide mutase | protein | 159 | 47% helix, 16% strand | Q2QJL3 |
| B | N5-carboxyaminoimidazole ribonucleotide mutase | protein | 161 | 47% helix, 16% strand | Q2QJL3 |
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 | 51 | 0.31 | 0.76 | 12 | empty |
| 2 | 56 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1647 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2FWA · Structure of PurE (N5-carboxyaminoimidazole ribonucleotide mutase) H89N from the… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q2QJL3
- Elsewhere: RCSB PDB 2FWA · PDBe 2FWA · UniProt Q2QJL3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.