8DGO: Growth Factor Receptor-Bound Protein 2

Growth Factor Receptor-Bound Protein 2 (Grb2) bound to phosphorylated PEAK3 (pY24) peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Jun 2023.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,679
Mol. weight: 51.67 kDa
Released: 7 Jun 2023

Explore 8DGO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8DGO contains 17 α-helices and 50 β-strands across 2 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: 8 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	1-5	5	1
β-strand	9	1	2
β-strand	16	1	1
β-strand	19	1	2
β-strand	24-27	4	1
α-helix	28	1
β-strand	33	1	1
β-strand	36-41	6	1
β-strand	44-49	6	1
α-helix	50-52	3
β-strand	53-55	3	1
α-helix	56-58	3
β-strand	61	1	3
α-helix	67-75	9
β-strand	82-87	6	3
β-strand	95-101	7	3
β-strand	104-110	7	3
β-strand	111-112	2	4
β-strand	118-119	2	4
β-strand	124-125	2	4
α-helix	128-137	10
β-strand	149-150	2	3
α-helix	157-159	3
β-strand	160-163	4	5
β-strand	167	1	6
β-strand	174	1	5
α-helix	175-176	2
β-strand	177	1	6
β-strand	182-187	6	5
β-strand	193-198	6	5
β-strand	201-206	6	5
α-helix	207-209	3
β-strand	210-213	4	5

Chain B: 9 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	1-5	5	7
β-strand	9	1	8
β-strand	16	1	7
β-strand	19	1	8
β-strand	24-27	4	7
β-strand	33	1	7
β-strand	36-41	6	7
β-strand	44-49	6	7
α-helix	50-52	3
β-strand	53-55	3	7
α-helix	56-58	3
β-strand	61	1	9
α-helix	67-75	9
β-strand	82-87	6	9
β-strand	95-101	7	9
β-strand	104-110	7	9
β-strand	111-112	2	10
β-strand	118-119	2	10
β-strand	125	1	10
α-helix	128-134	7
β-strand	149-150	2	9
α-helix	151-153	3
α-helix	155-156	2
α-helix	158-159	2
β-strand	160-163	4	11
β-strand	167	1	12
β-strand	174	1	11
α-helix	175-176	2
β-strand	177	1	12
β-strand	182-187	6	11
β-strand	193-198	6	11
β-strand	201-206	6	11
α-helix	207-209	3
β-strand	210-213	4	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth factor receptor bound protein 2	A, B	protein	219	Homo sapiens	P62993 (AlphaFold model)
Phosphorylated PEAK3 (pY24) peptide	C	protein	7	Homo sapiens	Q6ZS72 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8DGO_1 Growth factor receptor bound protein 2 (chains A, B)
GSMEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPH
PWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKY
FLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFR
RGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV

Sequence of entity 2 (C), FASTA

>8DGO_2 Phosphorylated PEAK3 (pY24) peptide (chains C)
TYSNLGQ

Primary citation

Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling. Roy, M.J., Surudoi, M.G., Kropp, A. et al. Nat Commun (2023) 14:3542-3542. DOI 10.1038/s41467-023-38869-9 · PubMed

Other PDB entries of the same protein (UniProt P62993 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ICG 1.15 Å, Grb2 SH2 domain in phosphopeptide free form
3WA4 1.35 Å, Grb2 SH2 domain/CD28-derived peptide complex
1JYR 1.55 Å, Xray Structure of Grb2 SH2 Domain Complexed with a Phosphorylated Peptide
2VWF 1.58 Å, Grb2 SH3C (2)
2VVK 1.6 Å, Grb2 SH3C (1)
3OV1 1.6 Å, Crystal Structure of the Grb2 SH2 Domain in Complex with a pYXN-Derived Tripeptide
4P9V 1.64 Å, Grb2 SH2 complexed with a pTyr-Ac6cN-Asn tripeptide
1GCQ 1.68 Å, Crystal structure of vav and GRB2 SH3 domains
2W0Z 1.7 Å, Grb2 SH3C (3)
3C7I 1.7 Å, X-RAY crystal structure of the complex between the grb2-sh2 domain and a flexible…
3IN8 1.7 Å, Crystal Structure of the Grb2 SH2 Domain in Complex with a Flexible Ac-pTyr-Ile-Asn-NH2…
3S8L 1.71 Å, Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing…

Browse structure collections

About this viewer

MolViewer shows 8DGO 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.