Research workbench
The structural analysis of A.MUCINIPHILA sulfatase
Analyse The structural analysis of A.MUCINIPHILA sulfatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EBP
- Type
- protein
- Length
- 1,048 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfatase
- UniProt
- B2UR15
- Ligands
- CA
- Pockets
- 11 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfatase | protein | 526 | 35% helix, 15% strand | B2UR15 |
| B | Sulfatase | protein | 522 | 36% helix, 16% strand | B2UR15 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.46 | 0.76 | 32 | GOL |
| 2 | 152 | 0.44 | 0.76 | 29 | GOL |
| 3 | 87 | 0.35 | 0.75 | 13 | empty |
| 4 | 83 | 0.34 | 0.75 | 13 | empty |
| 5 | 70 | 0.34 | 0.76 | 14 | empty |
Compared structures
- 7EBP · The structural analysis of A.Muciniphila sulfatase · 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 B2UR15
- Elsewhere: RCSB PDB 7EBP · PDBe 7EBP · UniProt B2UR15
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