Research workbench
Crystal structure of the R132K:Y134F:R111L:L121D:T54V mutant of cellular retinoic acid-binding protein II at 1.51 ångström resolution
Analyse Crystal structure of the R132K:Y134F:R111L:L121D:T54V mutant of cellular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FEK
- 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
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Cellular retinoic acid-binding protein 2 | protein | 137 | 12% helix, 55% strand | P29373 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.80 | 0.88 | 43 | PEG |
| 2 | 653 | 0.75 | 0.81 | 55 | empty |
| 3 | 73 | 0.28 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- B–A · 58 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FEK · Crystal structure of the R132K:Y134F:R111L:L121D:T54V mutant of cellular retinoic… · the same entry in another collection · chain B against B, 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 3FEK · PDBe 3FEK · UniProt P29373
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