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Crystal structure of bacteroides thetaiotaomicron BT_3980, protein with actin-like ATPase fold and unknown function (NP_812891.1) from bacteroides thetaiotaomicron vpi-5482 at 1.85 a resolution
Analyse Crystal structure of bacteroides thetaiotaomicron BT_3980, protein with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HRG
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein BT_3980 with actin-like ATPase fold
- UniProt
- Q8A0P1
- Ligands
- UNL
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein BT_3980 with actin-like ATPase fold | protein | 257 | 34% helix, 33% strand | Q8A0P1 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.55 | 0.79 | 27 | UNL |
| 2 | 77 | 0.47 | 0.83 | 20 | empty |
| 3 | 113 | 0.45 | 0.78 | 28 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 3HRG · Crystal structure of Bacteroides thetaiotaomicron BT_3980, protein with actin-like ATPase… · 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 Q8A0P1
- Elsewhere: RCSB PDB 3HRG · PDBe 3HRG · UniProt Q8A0P1
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