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Crystal structure of a putative ATPase (CHU_0153) from cytophaga hutchinsonii atcc 33406 at 2.00 a resolution
Analyse Crystal structure of a putative ATPase (CHU_0153) from cytophaga hutchinsonii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R44
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q11YS1
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 330 | 51% helix, 15% strand | Q11YS1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.44 | 0.77 | 23 | empty |
| 2 | 137 | 0.38 | 0.73 | 24 | PG4 |
| 3 | 66 | 0.31 | 0.75 | 13 | PG4 |
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2R44 · Crystal structure of a putative ATPase (CHU_0153) from cytophaga hutchinsonii atcc 33406… · 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 Q11YS1
- Elsewhere: RCSB PDB 2R44 · PDBe 2R44 · UniProt Q11YS1
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