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Structure of human mcl-1 in complex with puma BH3 peptide

Analyse Structure of human mcl-1 in complex with puma BH3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QFM
Type: protein
Length: 159 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-binding component 3
UniProt: Q07820, Q9BXH1
Ligands: ZN, CL

Structure

x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Induced myeloid leukemia cell differentiation protein mcl- 1	protein	140	83% helix, 0% strand	Q07820
B	BCL-2-binding component 3	protein	19	89% helix, 0% strand	Q9BXH1

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A, B
CL · Chloride ion · ion · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 927 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6QFM · Structure of human Mcl-1 in complex with PUMA BH3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q9BXH1 · AlphaFold monomer V2.0 prediction for BCL-2-binding component 3, isoforms 1/2 (Q9BXH1) · a predicted model of the same protein · chain B against A, TM-score 0.72

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 Q9BXH1
Elsewhere: RCSB PDB 6QFM · PDBe 6QFM · UniProt Q07820 · UniProt Q9BXH1

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