1DDB: Mouse bid, NMR, 20 structures

Structure of mouse bid, NMR, 20 structures. Determined by solution NMR. Released 30 Aug 1999.

Method: Solution NMR
Organism: Mus musculus
Chains: 1
Atoms: 1,536
Mol. weight: 21.97 kDa
Released: 30 Aug 1999

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

Secondary structure: helices and β-sheets

1DDB contains 11 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	15-27	13
α-helix	32-39	8
α-helix	72-74	3
α-helix	83-97	15
α-helix	98-100	3
α-helix	106-113	8
α-helix	125-137	13
α-helix	141-145	5
α-helix	146-162	17
α-helix	167-180	14
α-helix	185-192	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (BID)	A	protein	195	Mus musculus	P70444 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1DDB_1 PROTEIN (BID) (chains A)
MDSEVSNGSGLGAKHITDLLVFGFLQSSGCTRQELEVLGRELPVQAYWEADLEDELQTDG
SQASRSFNQGRIEPDSESQEEIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSE
EDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFHTTVNFINQ
NLFSYVRNLVRNEMD

Primary citation

Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. McDonnell, J.M., Fushman, D., Milliman, C.L. et al. Cell (1999) 96:625-634. DOI 10.1016/S0092-8674(00)80573-5 · PubMed

Other PDB entries of the same protein (UniProt P70444 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VOI 2.1 Å, Structure of mouse A1 bound to the Bid BH3-domain

Browse structure collections

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