Research workbench
Crystal structure of a putative hydrolase (BT_2193) from bacteroides thetaiotaomicron vpi-5482 at 1.25 a resolution
Analyse Crystal structure of a putative hydrolase (BT_2193) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SGG
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical hydrolase
- UniProt
- Q8A5P5
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical hydrolase | protein | 512 | 39% helix, 19% strand | Q8A5P5 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.58 | 0.81 | 26 | GOL |
| 2 | 76 | 0.42 | 0.80 | 22 | empty |
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 3SGG · Crystal structure of a putative hydrolase (BT_2193) from Bacteroides thetaiotaomicron… · 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 Q8A5P5
- Elsewhere: RCSB PDB 3SGG · PDBe 3SGG · UniProt Q8A5P5
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