6BCR: 14-3-3 protein theta

Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T340. Determined by X-ray diffraction at 1.99 Å resolution. Released 24 Oct 2018.

Method: X-ray diffraction
Resolution: 1.99 Å
Organism: Homo sapiens
Chains: 8
Atoms: 8,477
Mol. weight: 119.23 kDa
Ligands: MG, ETF
Released: 24 Oct 2018

Explore 6BCR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6BCR contains 57 α-helices and 0 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-16	14
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-68	31
α-helix	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	136-159	24
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	208-228	21

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-67	30
α-helix	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	202-205	4
α-helix	208-228	21

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	343-344	2

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-16	14
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-67	30
α-helix	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-203	19
α-helix	208-228	21

Chain F: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-32	14
α-helix	34-36	3
α-helix	38-67	30
α-helix	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	208-228	21

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	337-339	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein theta	A, B, E, F	protein	245	Homo sapiens	P27348 (AlphaFold model)
Insulin receptor substrate protein of 53 kDa, peptide (IRSp53)	C, D, G, H	protein	14	Homo sapiens	Q9UQB8 (AlphaFold model)

Sequence of entity 1 (A, B, E, F), FASTA

>6BCR_1 14-3-3 protein theta (chains A, B, E, F)
MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWR
VISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLK
MKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYE
ILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAA
EGAEN

Sequence of entity 2 (C, D, G, H), FASTA

>6BCR_2 Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) (chains C, D, G, H)
LSDSYSNTLPVRKS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ETF	Trifluoroethanol	C2 H3 F3 O	2

Water and common crystallization additives (PEG, 1PE, EDO) are not listed.

Primary citation

Mechanism of IRSp53 inhibition by 14-3-3. Kast, D.J., Dominguez, R. Nat Commun (2019) 10:483-483. DOI 10.1038/s41467-019-08317-8 · PubMed

Other PDB entries of the same protein (UniProt P27348 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KZG 2.0 Å, 14-3-3 protein in Complex with CIC S301 phosphorylated peptide
6BCY 2.3 Å, Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T360
6BD1 2.35 Å, Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at S366
5IQP 2.6 Å, 14-3-3 protein tau isoform
6KZH 2.65 Å, 14-3-3 protein in Complex with CIC S173 phosphorylated peptide
2BTP 2.8 Å, 14-3-3 Protein Theta (Human) Complexed to Peptide
6BQT 2.8 Å, Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360
6BD2 2.9 Å, Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366

Browse structure collections

About this viewer

MolViewer shows 6BCR directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.