Research workbench
Cis-mutant R349A of the central aaa+ domain of the flagellar regulatory protein flrc
Analyse Cis-mutant R349A of the central aaa+ domain of the flagellar regulatory protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LUA
- Type
- protein
- Length
- 1,726 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar regulatory protein C
- UniProt
- A0A0H3AHP1
- Pockets
- 19 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, F | Flagellar regulatory protein C | protein | 247 | 44% helix, 14% strand | A0A0H3AHP1 |
| D, E, G | Flagellar regulatory protein C | protein | 246 | 45% helix, 14% strand | A0A0H3AHP1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B, C, D, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.79 | 0.81 | 101 | EDO |
| 2 | 1060 | 0.79 | 0.80 | 97 | EDO |
| 3 | 1122 | 0.78 | 0.80 | 102 | EDO |
| 4 | 1115 | 0.78 | 0.80 | 102 | EDO |
| 5 | 1026 | 0.77 | 0.79 | 93 | EDO |
Interfaces
7 interfaces between chains.
- D–E · 933 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 921 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 890 Ų buried · 15 hydrogen bonds · protein-protein
- F–G · 879 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 874 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6LUA · Cis-mutant R349A of the central AAA+ domain of the flagellar regulatory protein FlrC · 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 A0A0H3AHP1
- Elsewhere: RCSB PDB 6LUA · PDBe 6LUA · UniProt A0A0H3AHP1
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