Research workbench
Structure of human mcl-1 in complex with bim BH3 peptide
Analyse Structure of human mcl-1 in complex with bim BH3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QFI
- Type
- protein
- Length
- 170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Induced myeloid leukemia cell differentiation protein mcl- 1; BCL-2-like protein 11
- UniProt
- Q07820, O43521
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Induced myeloid leukemia cell differentiation protein mcl- 1 | protein | 147 | 74% helix, 0% strand | Q07820 |
| B | BCL-2-like protein 11 | protein | 23 | 87% helix, 0% strand | O43521 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · 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 | 61 | 0.31 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1063 Ų buried · 13 hydrogen bonds · protein-protein
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 Q07820
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 6QFI · PDBe 6QFI · UniProt Q07820 · UniProt O43521
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