Research workbench
Crystal structure of RBBP9 in complex with phenylalanine
Analyse Crystal structure of RBBP9 in complex with phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OEX
- Type
- protein
- Length
- 376 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine hydrolase RBBP9
- EC
- 3.-.-.-
- UniProt
- O75884
- Ligands
- PHE
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydrolase RBBP9 (EC 3.-.-.-) | protein | 192 | 33% helix, 17% strand | O75884 |
| B | Serine hydrolase RBBP9 (EC 3.-.-.-) | protein | 184 | 35% helix, 17% strand | O75884 |
Ligands and binding sites
- PHE · Phenylalanine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.51 | 0.75 | 28 | empty |
| 2 | 115 | 0.48 | 0.80 | 27 | PHE |
| 3 | 110 | 0.47 | 0.79 | 29 | PHE |
| 4 | 73 | 0.42 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 216 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 O75884
- Elsewhere: RCSB PDB 7OEX · PDBe 7OEX · UniProt O75884
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.