MolNFT v1 · #106148 · protein
Crystal structure of the semet BICC1 SAM domain R924E mutant
4RQM · Protein bicaudal C homolog 1: “Crystal structure of the semet BICC1 SAM domain R924E mutant”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.40). MolNFT v1 #106148 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4RQM
- Type
- protein
- Length
- 184 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein bicaudal C homolog 1
- UniProt
- Q9H694
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 3 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein bicaudal C homolog 1 | protein | 63 | 73% helix, 0% strand | Q9H694 |
| B | Protein bicaudal C homolog 1 | protein | 59 | 73% helix, 0% strand | Q9H694 |
| C | Protein bicaudal C homolog 1 | protein | 62 | 66% helix, 0% strand | Q9H694 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
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 | 55 | 0.40 | 0.81 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 346 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 344 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4RQM · Crystal structure of the SeMET BICC1 SAM Domain R924E mutant · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H694 · AlphaFold monomer V2.0 prediction for protein bicaudal C homolog 1 (Q9H694) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q9H694
- Elsewhere: RCSB PDB 4RQM · PDBe 4RQM · UniProt Q9H694
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