4C69: PDB entry 4C69

ATP binding to murine voltage-dependent anion channel 1 (mVDAC1). Determined by X-ray diffraction at 2.28 Å resolution. Released 4 Jun 2014.

Method: X-ray diffraction
Resolution: 2.28 Å
Organism: MUS MUSCULUS
Chains: 1
Atoms: 2,409
Mol. weight: 35.44 kDa
Ligands: LDA, MC3, ATP
Released: 4 Jun 2014

Explore 4C69 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C69 contains 3 α-helices and 19 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 X: 3 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	12-19	8
β-strand	26-32	7	1
β-strand	38-48	11	1
β-strand	54-64	11	1
β-strand	69-76	8	1
β-strand	81-88	8	1
β-strand	95-103	9	1
β-strand	110-120	11	1
β-strand	123-132	10	1
β-strand	135-146	12	1
β-strand	149-158	10	1
β-strand	163-174	12	1
β-strand	178-185	8	1
β-strand	189-199	11	1
β-strand	202-211	10	1
β-strand	217-228	12	1
β-strand	231-238	8	1
β-strand	242-252	11	1
β-strand	255-264	10	1
α-helix	265-267	3
β-strand	274-282	9	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Voltage-dependent anion-selective channel protein 1	X	protein	295	MUS MUSCULUS	Q60932 (AlphaFold model)

Sequence of entity 1 (X), FASTA

>4C69_1 VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1 (chains X)
MRGSHHHHHHGSMAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSAN
TETTKVNGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTG
KKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETSKSRVTQSN
FAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQVD
PDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA

Ligands and cofactors

ID	Name	Formula	Copies
LDA	Lauryl dimethylamine-N-oxide	C14 H31 N O	6
MC3	1,2-dimyristoyl-rac-glycero-3-phosphocholine	C36 H72 N O8 P	2
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

Structure-Guided Simulations Illuminate the Mechanism of ATP Transport Through Vdac1. Choudhary, O.P., Paz, A., Adelman, J.L. et al. Nat Struct Mol Biol (2014) 21:626. DOI 10.1038/NSMB.2841 · PubMed

Other PDB entries of the same protein (UniProt Q60932 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3EMN 2.3 Å, The Crystal Structure of Mouse VDAC1 at 2.3 A resolution
9GNG 2.4 Å, mouse VDAC1 in complex with MPD
7TCV 2.6 Å, VDAC K12E mutant
7KUH 3.12 Å, MicroED structure of mVDAC

Browse structure collections

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