Research workbench
Crystal structure of apo-cellular retinoic acid binding protein type II at 1.35 ångströms resolution
Analyse Crystal structure of apo-cellular retinoic acid binding protein type II at 1.35… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FS6
- Type
- protein
- Length
- 273 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, CL
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular retinoic acid-binding protein 2 | protein | 136 | 13% helix, 55% strand | P29373 |
| B | Cellular retinoic acid-binding protein 2 | protein | 137 | 12% helix, 54% strand | P29373 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · chains B
- ACT · Acetate ion · additive · 7 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 | 356 | 0.77 | 0.87 | 42 | ACT |
| 2 | 521 | 0.70 | 0.79 | 53 | CL, ACT |
Interfaces
1 interface between chains.
- A–B · 29 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2FS6 · Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II At 1.35 Angstroms… · 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 A against A, TM-score 0.99
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 2FS6 · PDBe 2FS6 · UniProt P29373
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