MolNFT v1 · #69156 · protein
Crystal structure of murine ig-beta (CD79B) homodimer
3KHO · B-cell antigen receptor complex-associated protein beta…: “Crystal structure of murine ig-beta (CD79B) homodimer”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.27). MolNFT v1 #69156 on GenesisL1: 3D structure…
- PDB
- 3KHO
- Type
- protein
- Length
- 183 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- B-cell antigen receptor complex-associated protein beta chain
- UniProt
- P15530
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B-cell antigen receptor complex-associated protein beta chain | protein | 88 | 3% helix, 51% strand | P15530 |
| B | B-cell antigen receptor complex-associated protein beta chain | protein | 95 | 6% helix, 55% strand | P15530 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B, A
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 | 60 | 0.27 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 579 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3KHO · Crystal structure of murine Ig-beta (CD79b) homodimer · the same entry in another collection · chain A against A, TM-score 1.00
- P15530 · AlphaFold monomer V2.0 prediction for B-cell antigen receptor complex-associated protein… · a predicted model of the same protein · chain A 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 P15530
- Elsewhere: RCSB PDB 3KHO · PDBe 3KHO · UniProt P15530
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