1ST6: Cytoskeletal protein

Name: PDB 1ST6: Crystal structure of a cytoskeletal protein
Published: 2004-08-03
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell adhesion

Crystal structure of a cytoskeletal protein. Determined by X-ray diffraction at 3.1 Å resolution. Released 3 Aug 2004.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Gallus gallus
Chains: 1
Atoms: 8,055
Mol. weight: 117.51 kDa
Released: 3 Aug 2004

Explore 1ST6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ST6 contains 36 α-helices and 6 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: 36 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
α-helix	10-32	23
α-helix	41-61	21
α-helix	68-97	30
α-helix	104-146	43
α-helix	154-179	26
β-strand	182	1	1
α-helix	185-200	16
α-helix	202-217	16
α-helix	224-247	24
α-helix	256-275	20
α-helix	277-285	9
α-helix	296-311	16
α-helix	318-337	20
α-helix	338-342	5
α-helix	347-395	49
α-helix	405-421	17
α-helix	428-451	24
α-helix	457-482	26
α-helix	493-505	13
α-helix	516-531	16
α-helix	535-556	22
α-helix	567-598	32
α-helix	604-614	11
α-helix	622-650	29
α-helix	654-681	28
α-helix	689-714	26
α-helix	719-739	21
α-helix	752-772	21
α-helix	777-802	26
α-helix	814-817	4
α-helix	824-835	12
α-helix	897-909	13
β-strand	912	1	2
α-helix	918-935	18
α-helix	945-971	27
β-strand	972	1	3
α-helix	975-985	11
α-helix	988-1004	17
α-helix	1013-1044	32
β-strand	1048	1	3
β-strand	1060	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vinculin	A	protein	1069	Gallus gallus	P12003 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ST6_1 Vinculin (chains A)
VPRMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRV
GKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILS
GTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDE
RQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKM
SAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQ
AIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRARGQGATPMAMQKAQQVS
QGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNGGSEGEEHIRGIMSEARK
VAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEARALAKQIATSLQNLQSKT
NRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGRRLANVMMGPY
RQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSLKDLKARMQEAMTQEVSD
VFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARLGATAEKAAAVGTANKTT
VEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAI
DTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRANRILLVAKREVENSEDP
KFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQP
QEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEAINQP
MMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKA
SDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESE
QATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ

Primary citation

Structural basis for vinculin activation at sites of cell adhesion. Bakolitsa, C., Cohen, D.M., Bankston, L.A. et al. Nature (2004) 430:583-586. DOI 10.1038/nature02610 · PubMed

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
6NR7 3.0 Å, Rerefinement of chicken vinculin

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