1BHI: Cre-BP1

Structure of transactivation domain of cre-BP1/ATF-2, NMR, 20 structures. Determined by solution NMR. Released 15 Jun 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
302
Mol. weight
4.34 kDa
Released
15 Jun 1999

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

Secondary structure: helices and β-sheets

1BHI contains 1 α-helix and 2 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: 1 helix, 2 β-strands

ElementResiduesLengthSheet
β-strand7-821
β-strand17-1821
α-helix21-3212

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cre-BP1Aprotein38Homo sapiensP15336 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1BHI_1 CRE-BP1 (chains A)
MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFG

Primary citation

Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain. Nagadoi, A., Nakazawa, K., Uda, H. et al. J Mol Biol (1999) 287:593-607. DOI 10.1006/jmbi.1999.2620 · PubMed

Other PDB entries of the same protein (UniProt P15336 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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