Research workbench
Crystal structure of a putative glycosylhydrolase (BT_3782) from bacteroides thetaiotaomicron vpi-5482 at 1.89 a resolution
Analyse Crystal structure of a putative glycosylhydrolase (BT_3782) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MU9
- Type
- protein
- Length
- 719 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase family 73
- UniProt
- Q8A184
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase family 73 | protein | 360 | 58% helix, 9% strand | Q8A184 |
| B | Glycoside hydrolase family 73 | protein | 359 | 58% helix, 11% strand | Q8A184 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 16 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1106 | 0.86 | 0.86 | 88 | EDO, EPE |
| 2 | 221 | 0.63 | 0.82 | 31 | EDO |
| 3 | 226 | 0.62 | 0.82 | 28 | empty |
| 4 | 187 | 0.57 | 0.80 | 29 | EDO, EPE |
| 5 | 223 | 0.49 | 0.75 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 676 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4MU9 · Crystal structure of a putative glycosylhydrolase (BT_3782) from Bacteroides… · 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 Q8A184
- Elsewhere: RCSB PDB 4MU9 · PDBe 4MU9 · UniProt Q8A184
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