2AOB: High-affinity macrocyclic peptide mimetic

Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Oct 2005.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,036
Mol. weight: 55.36 kDa
Ligands: S1S
Released: 4 Oct 2005

Explore 2AOB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AOB contains 9 α-helices and 35 β-strands across 4 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: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	61	1	1
α-helix	67-75	9
β-strand	82	1	2
β-strand	83-87	5	1
β-strand	95-101	7	1
β-strand	104-109	6	1
β-strand	111-112	2	3
β-strand	118-119	2	3
β-strand	125	1	4
α-helix	128-137	10
β-strand	149	1	5

Chain B: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	61	1	6
α-helix	67-74	8
β-strand	82	1	5
β-strand	83-87	5	6
β-strand	95-101	7	6
β-strand	104-109	6	6
α-helix	110	1
β-strand	111-112	2	4
β-strand	118-119	2	4
β-strand	125	1	3
α-helix	128-135	8
β-strand	149	1	2

Chain C: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	61	1	7
α-helix	67-75	9
β-strand	82-87	6	7
β-strand	95-101	7	7
β-strand	104-109	6	7
β-strand	111-112	2	8
β-strand	118-119	2	8
β-strand	125	1	9
α-helix	128-134	7
β-strand	149	1	10

Chain D: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	61	1	11
α-helix	67-75	9
β-strand	82	1	10
β-strand	83-87	5	11
β-strand	95-101	7	11
β-strand	104-110	7	11
β-strand	111-112	2	9
β-strand	118-119	2	9
β-strand	125	1	8
α-helix	128-135	8
β-strand	149-150	2	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth factor receptor-bound protein 2	A, B, C, D	protein	99	Homo sapiens	P62993 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2AOB_1 Growth factor receptor-bound protein 2 (chains A, B, C, D)
MKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDG
AGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQ

Ligands and cofactors

ID	Name	Formula	Copies
S1S	2-(4-((9S,10S,14S,Z)-18-(2-amino-2-oxoethyl)-9-(carboxymethyl)-14-(naphthalen-1…	C41 H46 N4 O10	12

Primary citation

Crystal Structures of a High-affinity Macrocyclic Peptide Mimetic in Complex with the Grb2 SH2 Domain. Phan, J., Shi, Z.D., Burke, T.R. et al. J Mol Biol (2005) 353:104-115. DOI 10.1016/j.jmb.2005.08.037 · 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…

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