Research workbench
Crystal structure of putative cell adhesion protein (YP_001304840.1) from parabacteroides distasonis atcc 8503 at 2.05 a resolution
Analyse Crystal structure of putative cell adhesion protein (YP_001304840.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LIU
- Type
- protein
- Length
- 745 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell adhesion protein
- UniProt
- A6LHQ4
- Ligands
- CL, SO4
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cell adhesion protein | protein | 372 | 6% helix, 45% strand | A6LHQ4 |
| B | Putative cell adhesion protein | protein | 373 | 6% helix, 45% strand | A6LHQ4 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains B
- EDO · 1,2-ethanediol · additive · 5 copies · chains B, A
- GOL · Glycerol · additive · 2 copies · chains A, B
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 | 881 | 0.77 | 0.80 | 90 | GOL, EDO |
| 2 | 68 | 0.43 | 0.81 | 18 | empty |
| 3 | 68 | 0.41 | 0.80 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 537 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3LIU · Crystal structure of Putative cell adhesion protein (YP_001304840.1) from Parabacteroides… · 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 A6LHQ4
- Elsewhere: RCSB PDB 3LIU · PDBe 3LIU · UniProt A6LHQ4
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