1BMB: GRB2-SH2 domain

GRB2-SH2 domain in complex with kpfy*vnvef (PKF270-974). Determined by X-ray diffraction at 1.8 Å resolution. Released 29 Jul 1998.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
2
Atoms
1,018
Mol. weight
15.57 kDa
Released
29 Jul 1998

Explore 1BMB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BMB contains 2 α-helices and 9 β-strands across 1 chain. 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

ElementResiduesLengthSheet
β-strand6111
α-helix67-759
β-strand8212
β-strand83-8751
β-strand95-10171
β-strand104-10961
β-strand111-11223
β-strand118-11923
β-strand124-12523
α-helix128-1347
β-strand14912

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (growth factor receptor bound protein 2)Aprotein123Homo sapiensP62993 (AlphaFold model)
Protein (PKF270-974)Iprotein9
Sequence of entity 1 (A), FASTA
>1BMB_1 PROTEIN (GROWTH FACTOR RECEPTOR BOUND PROTEIN 2) (chains A)
MGSPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDV
QHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALF
DFD
Sequence of entity 2 (I), FASTA
>1BMB_2 PROTEIN (PKF270-974) (chains I)
KPFYVNVEF

Primary citation

Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1). Ettmayer, P., France, D., Gounarides, J. et al. J Med Chem (1999) 42:971-980. DOI 10.1021/jm9811007 · PubMed

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

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