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Human bfl-1 in complex with a bfl-1-specific selected peptide

Analyse Human bfl-1 in complex with a bfl-1-specific selected peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UUK
Type: protein
Length: 174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-related protein A1; Bfl-1-specific selected peptide
UniProt: Q16548
Ligands: ACE, SO4

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-related protein A1	protein	152	74% helix, 0% strand	Q16548
B	Bfl-1-specific selected peptide	protein	22	91% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains B
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 915 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5UUK · Human Bfl-1 in complex with a Bfl-1-specific selected peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q16548 · AlphaFold monomer V2.0 prediction for BCL-2-related protein A1 (Q16548) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q16548
Elsewhere: RCSB PDB 5UUK · PDBe 5UUK · UniProt Q16548

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