Research workbench
Structure of the epididymal retinoic acid-binding protein at 2.1 ångströms resolution
Analyse Structure of the epididymal retinoic acid-binding protein at 2.1 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EPA
- Type
- protein
- Length
- 324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epididymal retinoic acid-binding protein
- UniProt
- P06911
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epididymal retinoic acid-binding protein | protein | 160 | 18% helix, 49% strand | P06911 |
| B | Epididymal retinoic acid-binding protein | protein | 164 | 18% helix, 43% strand | P06911 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.74 | 0.83 | 42 | empty |
| 2 | 415 | 0.73 | 0.83 | 53 | empty |
| 3 | 310 | 0.69 | 0.83 | 40 | empty |
| 4 | 58 | 0.34 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 707 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1EPA · Structure of the epididymal retinoic acid-binding protein at 2.1 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P06911 · AlphaFold monomer V2.0 prediction for epididymal-specific lipocalin-5 (P06911) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P06911
- Elsewhere: RCSB PDB 1EPA · PDBe 1EPA · UniProt P06911
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