Research workbench
Crystal structure of a GH5_18 from bifidobacterium longum subsp. infantis
Analyse Crystal structure of a GH5_18 from bifidobacterium longum subsp. infantis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LQX
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase BLGH5_18
- UniProt
- B7GNS6
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase BLGH5_18 | protein | 420 | 42% helix, 15% strand | B7GNS6 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 342 | 0.62 | 0.78 | 32 | EDO |
| 2 | 115 | 0.48 | 0.80 | 26 | empty |
| 3 | 106 | 0.38 | 0.75 | 22 | empty |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 7LQX · Crystal structure of a GH5_18 from Bifidobacterium longum subsp. infantis · 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 B7GNS6
- Elsewhere: RCSB PDB 7LQX · PDBe 7LQX · UniProt B7GNS6
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