Research workbench
Crystal structure of human mcl-1 in complex with modified bim BH3 peptide sah-MS1-18
Analyse Crystal structure of human mcl-1 in complex with modified 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
- 5W89
- Type
- protein
- Length
- 161 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Induced myeloid leukemia cell differentiation protein mcl- 1; Modified bim BH3 peptide…
- UniProt
- Q07820
- Ligands
- ACE, ZN
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Induced myeloid leukemia cell differentiation protein mcl- 1 | protein | 141 | 82% helix, 0% strand | Q07820 |
| B | Modified bim BH3 peptide sah-MS1-18 | protein | 20 | 90% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 882 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 5W89 · Crystal structure of human Mcl-1 in complex with modified Bim BH3 peptide SAH-MS1-18 · the same entry in another collection · chain A against A, TM-score 1.00
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
- Elsewhere: RCSB PDB 5W89 · PDBe 5W89 · UniProt Q07820
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.