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Crystal structure of the R132K:R111L:T54E mutant of cellular retinoic acid-binding protein II at 1.85 ångström resolution
Analyse Crystal structure of the R132K:R111L:T54E 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
- 3FEL
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular retinoic acid-binding protein 2
- UniProt
- P29373
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cellular retinoic acid-binding protein 2 | protein | 137 | 12% helix, 55% strand | P29373 |
Ligands and binding sites
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 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 | 406 | 0.79 | 0.88 | 42 | B3P |
| 2 | 633 | 0.74 | 0.81 | 57 | B3P |
Interfaces
1 interface between chains.
- A–B · 34 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FEL · Crystal structure of the R132K:R111L:T54E 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 3FEL · PDBe 3FEL · UniProt P29373
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