Research workbench
Flah from sulfolobus acidocaldarius with ATP and mg-ion
Analyse Flah from sulfolobus acidocaldarius with ATP and mg-ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YDS
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagella-related protein H
- EC
- 3.6.1.3
- UniProt
- Q4J9K9
- Ligands
- ATP, MG
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagella-related protein H (EC 3.6.1.3) | protein | 226 | 37% helix, 26% strand | Q4J9K9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 66 | 0.33 | 0.75 | 14 | empty |
| 2 | 51 | 0.25 | 0.73 | 19 | ATP, MG |
Compared structures
- 4YDS · FlaH from Sulfolobus acidocaldarius with ATP and Mg-Ion · 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 Q4J9K9
- Elsewhere: RCSB PDB 4YDS · PDBe 4YDS · UniProt Q4J9K9
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