1GVD: C-myb R2 V103L mutant

Crystal structure of C-myb R2 V103L mutant. Determined by X-ray diffraction at 1.45 Å resolution. Released 3 Jul 2003.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: MUS MUSCULUS
Chains: 1
Atoms: 553
Mol. weight: 6.53 kDa
Released: 3 Jul 2003

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

Secondary structure: helices and β-sheets

1GVD contains 5 α-helices and 0 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	95-96	2
α-helix	97-110	14
α-helix	115-119	5
α-helix	127-133	7
α-helix	134-138	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myb proto-oncogene protein	A	protein	52	MUS MUSCULUS	P06876 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GVD_1 MYB PROTO-ONCOGENE PROTEIN (chains A)
LIKGPWTKEEDQRLIKLVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPE

Primary citation

Crystal Structure of C-Myb DNA-Binding Domain: Specific Na+ Binding and Correlation with NMR Structure. Tahirov, T.H., Morii, H., Uedaira, H. et al. To be published.

Other PDB entries of the same protein (UniProt P06876 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1GV5 1.58 Å, Crystal structure of C-myb R2
1GUU 1.6 Å, Crystal structure of C-myb R1
1GV2 1.68 Å, Crystal structure of C-myb R2R3
6DNQ 2.35 Å, HBZ77 in complex with KIX and c-Myb
1H89 2.45 Å, Crystal structure of ternary protein-DNA COMPLEX2
1H88 2.8 Å, Crystal structure of ternary protein-DNA COMPLEX1
6DMX 2.8 Å, HBZ56 in complex with KIX and c-Myb
1IDY Structure of myb transforming protein, NMR, minimized average structure
1IDZ Structure of myb transforming protein, NMR, 20 structures
1MBE Mouse C-myb DNA-binding domain repeat 1
1MBF Mouse C-myb DNA-binding domain repeat 1
1MBG Mouse C-myb DNA-binding domain repeat 2

Browse structure collections

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