MolNFT v1 · #157919 · protein
Structure of human pacrg-MEIG1 complex
6NEP · Parkin coregulated gene protein: “Structure of human pacrg-MEIG1 complex”. X-ray diffraction, 2 ligands (CL, PO4), 1 pocket (best druggability 0.38). MolNFT v1 #157919 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NEP
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Parkin coregulated gene protein; Meiosis expressed gene 1 protein homolog
- UniProt
- Q96M98, Q5JSS6
- Ligands
- CL, PO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parkin coregulated gene protein | protein | 170 | 67% helix, 1% strand | Q96M98 |
| B | Meiosis expressed gene 1 protein homolog | protein | 84 | 26% helix, 19% strand | Q5JSS6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.38 | 0.76 | 22 | CL |
Interfaces
1 interface between chains.
- A–B · 728 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6NEP · Structure of human PACRG-MEIG1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q96M98 · AlphaFold monomer V2.0 prediction for parkin coregulated gene protein (Q96M98) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q5JSS6 · AlphaFold monomer V2.0 prediction for meiosis expressed gene 1 protein homolog (Q5JSS6) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q96M98
- Every structure of UniProt Q5JSS6
- Elsewhere: RCSB PDB 6NEP · PDBe 6NEP · UniProt Q96M98 · UniProt Q5JSS6
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