Research workbench
Bacteroides intestinalis feruloyl esterase, BACINT_01033
Analyse Bacteroides intestinalis feruloyl esterase, BACINT_01033 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MOU
- Type
- protein
- Length
- 713 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoamylase N-terminal domain protein
- UniProt
- B3C969
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoamylase N-terminal domain protein | protein | 359 | 26% helix, 28% strand | B3C969 |
| B | Isoamylase N-terminal domain protein | protein | 354 | 26% helix, 28% strand | B3C969 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1116 | 0.81 | 0.82 | 90 | empty |
| 2 | 111 | 0.61 | 0.86 | 27 | empty |
| 3 | 104 | 0.48 | 0.80 | 26 | empty |
| 4 | 153 | 0.46 | 0.76 | 31 | empty |
| 5 | 142 | 0.42 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1906 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 6MOU · Bacteroides intestinalis feruloyl esterase, Bacint_01033 · 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 B3C969
- Elsewhere: RCSB PDB 6MOU · PDBe 6MOU · UniProt B3C969
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