Research workbench
Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) mutant H59N from the acidophilic bacterium acetobacter aceti, at pH 5.4
Analyse Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) mutant H59N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FW6
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N5-carboxyaminoimidazole ribonucleotide mutase
- UniProt
- Q2QJL3
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N5-carboxyaminoimidazole ribonucleotide mutase | protein | 159 | 48% helix, 14% strand | Q2QJL3 |
| B | N5-carboxyaminoimidazole ribonucleotide mutase | protein | 160 | 48% helix, 14% strand | Q2QJL3 |
Ligands and binding sites
- CIT · Citric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.34 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1633 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 2FW6 · Structure of PurE (N5-carboxyaminoimidazole ribonucleotide mutase) mutant H59N 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 2FW6 · PDBe 2FW6 · UniProt Q2QJL3
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