2C3E: The bovine mitochondrial ADP-ATP carrier

The bovine mitochondrial ADP-ATP carrier. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Oct 2005.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
BOS TAURUS
Chains
1
Atoms
2,515
Mol. weight
38.04 kDa
Ligands
CDL, CXT
Released
20 Oct 2005

Explore 2C3E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C3E contains 14 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: 14 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix8-3730
α-helix38-403
α-helix53-6412
α-helix66-705
α-helix73-9826
α-helix108-14134
α-helix156-17217
α-helix176-20025
α-helix210-22617
α-helix228-23811
α-helix253-2597
α-helix260-2645
α-helix268-2703
α-helix275-29016

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Adp/atp translocase 1Aprotein297BOS TAURUSP02722 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2C3E_1 ADP/ATP TRANSLOCASE 1 (chains A)
SDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRI
PKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGG
AAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSV
QGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQ
SGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV

Ligands and cofactors

IDNameFormulaCopies
CDLCardiolipinC81 H156 O17 P23
CXTCarboxyatractylosideC31 H46 O18 S21

Primary citation

Structural Basis for Lipid-Mediated Interactions between Mitochondrial Adp/ATP Carrier Monomers. Nury, H., Dahout-Gonzalez, C., Trezeguet, V. et al. FEBS Lett (2005) 579:6031. DOI 10.1016/J.FEBSLET.2005.09.061 · PubMed

Other PDB entries of the same protein (UniProt P02722 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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