MolNFT v1 · #37143 · protein
Crystal structure of the F15W mutant of apo-cellular retinoic acid binding protein type II at 1.51 ångströms resolution
2FRS · Cellular retinoic acid-binding protein 2: “Crystal structure of the F15W mutant of apo-cellular retinoic acid binding protein type II at 1.51 ångströms…”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.70). MolNFT…
- PDB
- 2FRS
- Type
- protein
- Length
- 257 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
- NA
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular retinoic acid-binding protein 2 | protein | 124 | 6% helix, 60% strand | P29373 |
| B | Cellular retinoic acid-binding protein 2 | protein | 133 | 14% helix, 54% strand | P29373 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A
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 | 348 | 0.70 | 0.83 | 29 | NA |
| 2 | 313 | 0.68 | 0.82 | 34 | empty |
| 3 | 68 | 0.29 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 195 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2FRS · Crystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type… · the same entry in another collection · chain A against A, TM-score 1.00
- P29373 · AlphaFold monomer V2.0 prediction for cellular retinoic acid-binding protein 2 (P29373) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 2FRS · PDBe 2FRS · UniProt P29373
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