MolNFT v1 · #147127 · protein

Human bfl-1 in complex with the bfl-1-specific designed peptide SRT.F4

6E3I · BCL-2-related protein A1: “Human bfl-1 in complex with the bfl-1-specific designed peptide SRT.F4”. X-ray diffraction, 3 ligands (ACE, NH2, SO4). MolNFT v1 #147127 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6E3I
Type: protein
Length: 173 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-related protein A1; Peptide SRT.F4
UniProt: Q16548
Ligands: ACE, NH2, SO4

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-related protein A1	protein	152	73% helix, 0% strand	Q16548
B	Peptide SRT.F4	protein	21	90% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains B
NH2 · Amino group · ion · chains A, B
SO4 · Sulfate ion · ion · 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 · 982 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

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

Compared structures

6E3I · Human Bfl-1 in complex with the Bfl-1-specific designed peptide srt.F4 · 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 6E3I · PDBe 6E3I · UniProt Q16548

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