Research workbench
Crystal structure of engineered protein, northeast structural genomics consortium target OR422
Analyse Crystal structure of engineered protein, northeast structural genomics… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LNY
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Engineered protein OR422
- Ligands
- CD, CL
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Engineered protein OR422 | protein | 248 | 41% helix, 15% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.61 | 0.92 | 19 | empty |
| 2 | 54 | 0.28 | 0.75 | 19 | CD |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4LNY · Crystal Structure of Engineered Protein, Northeast Structural Genomics Consortium Target… · 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
- Elsewhere: RCSB PDB 4LNY · PDBe 4LNY
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