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Crystal structure of the R132K:R111L:A32E mutant of cellular retinoic acid-binding protein II at 1.56 ångström resolution
Analyse Crystal structure of the R132K:R111L:A32E mutant of cellular retinoic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FEN
- Type
- protein
- Length
- 261 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular retinoic acid-binding protein 2
- UniProt
- P29373
- Ligands
- CL
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular retinoic acid-binding protein 2 | protein | 137 | 13% helix, 55% strand | P29373 |
| B | Cellular retinoic acid-binding protein 2 | protein | 124 | 6% helix, 61% strand | P29373 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 793 | 0.79 | 0.82 | 64 | CL |
| 2 | 347 | 0.74 | 0.85 | 34 | CL |
Interfaces
1 interface between chains.
- A–B · 83 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3FEN · Crystal structure of the R132K:R111L:A32E mutant of cellular retinoic acid-binding… · 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 P29373
- Elsewhere: RCSB PDB 3FEN · PDBe 3FEN · UniProt P29373
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