6NR7: Rerefinement of chicken vinculin

Rerefinement of chicken vinculin. Determined by X-ray diffraction at 3.0 Å resolution. Released 29 Jan 2020.

Method

X-ray diffraction

Resolution

3.0 Å

Organism

Gallus gallus

Chains

1

Atoms

8,443

Mol. weight

120.2 kDa

Ligands

PO4, KYG

Released

29 Jan 2020

Explore 6NR7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6NR7 contains 42 α-helices and 8 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: 42 helices, 8 β-strands

Molecules and chains

>6NR7_1 Vinculin (chains A)
MGSSHHHHHHSSGLVPRGSHMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDL
TAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPY
SVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTY
TKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKS
QGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQA
KGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRA
RGQGATPMAMQKAQQVSQGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNG
GSEGEEHIRGIMSEARKVAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEAR
ALAKQIATSLQNLQSKTNRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIR
GLVAEGRRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSL
KDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARL
GATAEKAAAVGTANKTTVEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKN
QWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRA
NRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDS
GYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEE
KDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGG
SGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILST
VKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVR
KTPWYQ

Ligands and cofactors

Water and common crystallization additives (SO4) are not listed.

Primary citation

Refined model of chicken vinculin suggests the mechanism of activation by helical super-bundle unfurling. Stec, D.L., Stec, B. To be published.

Related structures

Other PDB entries of the same protein (UniProt P12003 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 1QKR 1.8 Å, Crystal structure of the vinculin tail and a pathway for activation
• 1ZVZ 1.8 Å, Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844
• 1T01 2.06 Å, Vinculin complexed with the VBS1 helix from talin
• 1ZW2 2.1 Å, Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369
• 3ZDL 2.3 Å, Vinculin head (1-258) in complex with a RIAM fragment
• 4E17 2.3 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
• 1U6H 2.38 Å, Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)
• 4E18 2.4 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
• 1XWJ 2.6 Å, Vinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)
• 2GDC 2.74 Å, Structure of Vinculin VD1 / IpaA560-633 complex
• 6FQ4 2.89 Å, Structure of Chlamydial virulence factor TarP and vinculin head domain
• 1ST6 3.1 Å, Crystal structure of a cytoskeletal protein

Browse structure collections

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