5L0I: Vinculin

Human metavinculin MVt R975W cardiomyopathy-associated mutant (residues 959-1134). Determined by X-ray diffraction at 2.45 Å resolution. Released 31 Aug 2016.

Method
X-ray diffraction
Resolution
2.45 Å
Organism
Homo sapiens
Chains
1
Atoms
1,436
Mol. weight
19.76 kDa
Released
31 Aug 2016

Explore 5L0I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5L0I contains 5 α-helices 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix964-97714
β-strand98011
α-helix986-100419
α-helix1011-103929
α-helix1043-107533
α-helix1081-111434
β-strand112811

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
VinculinAprotein176Homo sapiensP18206 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5L0I_1 Vinculin (chains A)
NQPVNQPILAAAQSLHWEATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQC
AKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTN
ISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ

Primary citation

Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization. Chinthalapudi, K., Rangarajan, E.S., Brown, D.T. et al. Proc Natl Acad Sci U S A (2016) 113:9539-9544. DOI 10.1073/pnas.1600702113 · PubMed

Other PDB entries of the same protein (UniProt P18206 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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