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Structure of a single tryptophan mutant of acetobacter aceti pure containing 5-fluorotryptophan
Analyse Structure of a single tryptophan mutant of acetobacter aceti pure containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CTJ
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N5-carboxyaminoimidazole ribonucleotide mutase
- EC
- 5.4.99.18
- UniProt
- A0A063X4U8
- Ligands
- SO4, CL
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N5-carboxyaminoimidazole ribonucleotide mutase (EC 5.4.99.18) | protein | 158 | 47% helix, 15% strand | A0A063X4U8 |
| B | N5-carboxyaminoimidazole ribonucleotide mutase (EC 5.4.99.18) | protein | 161 | 45% helix, 16% strand | A0A063X4U8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1703 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 5CTJ · Structure of a single tryptophan mutant of Acetobacter aceti PurE containing… · 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 A0A063X4U8
- Elsewhere: RCSB PDB 5CTJ · PDBe 5CTJ · UniProt A0A063X4U8
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