Research workbench
Structure of the exo-L-galactose-6-sulfatase BUS1_11 from bacteroides uniformis
Analyse Structure of the exo-L-galactose-6-sulfatase BUS1_11 from bacteroides uniformis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LHA
- Type
- protein
- Length
- 1,000 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exo-L-galactose-6-sulfatase
- UniProt
- A0A4Y1VMZ7
- Ligands
- NI, CA
- Pockets
- 10 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-L-galactose-6-sulfatase | protein | 501 | 35% helix, 18% strand | A0A4Y1VMZ7 |
| B | Exo-L-galactose-6-sulfatase | protein | 499 | 33% helix, 18% strand | A0A4Y1VMZ7 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 4 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.55 | 0.74 | 37 | empty |
| 2 | 312 | 0.55 | 0.75 | 46 | empty |
| 3 | 216 | 0.51 | 0.76 | 25 | empty |
| 4 | 238 | 0.50 | 0.75 | 29 | empty |
| 5 | 197 | 0.50 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 898 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7LHA · Structure of the Exo-L-galactose-6-sulfatase BuS1_11 from Bacteroides uniformis · 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 A0A4Y1VMZ7
- Elsewhere: RCSB PDB 7LHA · PDBe 7LHA · UniProt A0A4Y1VMZ7
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