Research workbench
Crystal structure of aaa+/ sigma 54 activator domain of the flagellar regulatory protein flrc from vibrio cholerae in ATP analog bound state
Analyse Crystal structure of aaa+/ sigma 54 activator domain of the flagellar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QHT
- Type
- protein
- Length
- 1,722 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar regulatory protein C
- UniProt
- A5F6D4
- Ligands
- ANP, MG
- Pockets
- 14 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, G | Flagellar regulatory protein C | protein | 246 | 44% helix, 15% strand | A5F6D4 |
| B, F | Flagellar regulatory protein C | protein | 245 | 45% helix, 14% strand | A5F6D4 |
| C | Flagellar regulatory protein C | protein | 248 | 46% helix, 14% strand | A5F6D4 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 7 copies · chains A, B, C, D, E, F, G
- MG · Magnesium ion · metal · 7 copies · chains A, B, C, D, E, F, G
- EDO · 1,2-ethanediol · additive · 12 copies · chains A, G, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.80 | 0.82 | 100 | ANP, MG, EDO |
| 2 | 1174 | 0.79 | 0.81 | 99 | EDO, ANP, MG |
| 3 | 1075 | 0.78 | 0.80 | 104 | ANP, MG, EDO |
| 4 | 1139 | 0.78 | 0.80 | 105 | ANP, MG, EDO |
| 5 | 1181 | 0.77 | 0.79 | 102 | ANP, MG, EDO |
Interfaces
7 interfaces between chains.
- E–F · 848 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 845 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 838 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 834 Ų buried · 13 hydrogen bonds · protein-protein
- A–G · 824 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4QHT · Crystal structure of AAA+/ sigma 54 activator domain of the flagellar regulatory protein… · the same entry in another collection · chain C against C, 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 A5F6D4
- Elsewhere: RCSB PDB 4QHT · PDBe 4QHT · UniProt A5F6D4
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