3EMN: Mouse VDAC1

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution. Determined by X-ray diffraction at 2.3 Å resolution. Released 16 Dec 2008.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 1
Atoms: 2,250
Mol. weight: 32.87 kDa
Ligands: MC3
Released: 16 Dec 2008

Explore 3EMN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EMN contains 3 α-helices and 21 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, 21 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	7-9	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	95-104	10	1
β-strand	109-120	12	1
β-strand	123-131	9	1
β-strand	133	1	2
β-strand	135	1	2
β-strand	137-146	10	1
β-strand	149-158	10	1
β-strand	163-174	12	1
β-strand	178-185	8	1
β-strand	189-197	9	1
β-strand	202-211	10	1
β-strand	214-225	12	1
β-strand	231-238	8	1
β-strand	242-252	11	1
β-strand	255-264	10	1
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

>3EMN_1 Voltage-dependent anion-selective channel protein 1 (chains X)
MRGSHHHHHHGSMAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSAN
TETTKVNGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTG
KKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETSKSRVTQSN
FAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQVD
PDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA

Ligands and cofactors

ID	Name	Formula	Copies
MC3	1,2-dimyristoyl-rac-glycero-3-phosphocholine	C36 H72 N O8 P	1

Primary citation

The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Ujwal, R., Cascio, D., Colletier, J.P. et al. Proc Natl Acad Sci U S A (2008) 105:17742-17747. DOI 10.1073/pnas.0809634105 · PubMed

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

4C69 2.28 Å, ATP binding to murine voltage-dependent anion channel 1 (mVDAC1).
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

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3EMN is part of these collections:

Membrane proteins and transporters

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