MolNFT v1 · #44361 · protein
The NMR structure of the bid-bak complex
2M5B · BCL-2 homologous ANTAGONIST/KILLER: “The NMR structure of the bid-bak complex”. Solution nmr, 1 ligand (NH2), 1 pocket (best druggability 0.62). MolNFT v1 #44361 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2M5B
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2 homologous ANTAGONIST/KILLER; HUMAN_BID_BH3_SAHB
- UniProt
- Q16611
- Ligands
- NH2
- Pockets
- 1 · best druggability 0.62
Structure
solution nmr · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2 homologous ANTAGONIST/KILLER | protein | 169 | 66% helix, 0% strand | Q16611 |
| B | HUMAN_BID_BH3_SAHB | protein | 22 | 59% helix, 0% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.62 | 0.85 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 962 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
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 Q16611
- Elsewhere: RCSB PDB 2M5B · PDBe 2M5B · UniProt Q16611
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