MolNFT v1 · #137713 · protein
Bak in complex with bim-H3GLG
5VX0: “Bak in complex with bim-H3GLG”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #137713 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VX0
- Type
- protein
- Length
- 379 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16611, O43521
- Ligands
- MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 169 | — | Q16611 |
| B | — | protein | 25 | — | O43521 |
| C | — | protein | 161 | — | Q16611 |
| D | — | protein | 24 | — | O43521 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VX0 · Bak in complex with Bim-h3Glg · the same entry in another collection · chain D against D, TM-score 1.00
- Q16611 · AlphaFold monomer V2.0 prediction for BCL-2 homologous ANTAGONIST/KILLER (Q16611) · a predicted model of the same protein · chain C against A, TM-score 0.95
- O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain B against A, TM-score 0.80
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 Q16611
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 5VX0 · PDBe 5VX0 · UniProt Q16611 · UniProt O43521
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