7UTJ: Actin, alpha skeletal muscle

Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin. Determined by electron microscopy at 2.77 Å resolution. Released 8 Mar 2023.

Method: Electron microscopy
Resolution: 2.77 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 12
Atoms: 24,591
Mol. weight: 844.67 kDa
Ligands: ADP, MG
Released: 8 Mar 2023

Explore 7UTJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UTJ contains 180 α-helices and 118 β-strands across 12 chains. 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.

Chains A and D: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-38	4	2
β-strand	41-42	2	3
β-strand	53-54	2	2
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	81-87	7
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	5
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	335-337	3
α-helix	338-347	10
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chains B and C: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	29-32	4	7
β-strand	35-38	4	8
β-strand	41-42	2	9
β-strand	53-54	2	8
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	8
β-strand	71-72	2	10
β-strand	75-76	2	10
α-helix	81-87	7
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	7
α-helix	137-144	8
β-strand	150-155	6	11
β-strand	160-166	7	11
β-strand	169-170	2	11
α-helix	172-174	3
β-strand	176-178	3	11
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	12
β-strand	247-250	4	12
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-295	6
β-strand	297-300	4	11
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	11
α-helix	335-337	3
α-helix	338-347	10
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain E: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	23
β-strand	16-21	6	23
β-strand	29-32	4	23
β-strand	35-38	4	24
β-strand	53-54	2	24
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	24
β-strand	71-72	2	25
β-strand	75-76	2	25
α-helix	81-87	7
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	23
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	23
α-helix	137-144	8
β-strand	150-155	6	15
β-strand	160-166	7	15
β-strand	169-170	2	15
α-helix	172-174	3
β-strand	176-178	3	15
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	26
β-strand	247-250	4	26
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-295	6
β-strand	297-300	4	15
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	15
α-helix	335-337	3
α-helix	338-347	10
β-strand	357-358	2	23
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain F: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	27
β-strand	16-21	6	27
β-strand	29-32	4	27
β-strand	35-38	4	28
β-strand	53-54	2	28
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	28
β-strand	71-72	2	29
β-strand	75-76	2	29
α-helix	81-87	7
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	27
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	27
α-helix	137-144	8
β-strand	150-155	6	20
β-strand	160-166	7	20
β-strand	169-170	2	20
α-helix	172-174	3
β-strand	176-178	3	20
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	30
β-strand	247-250	4	30
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	20
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	20
α-helix	335-337	3
α-helix	338-347	10
β-strand	357-358	2	27
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chains G, H, I, K, L and Z: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	711-730	20
α-helix	739-765	27
α-helix	773-803	31
α-helix	812-842	31
α-helix	849-852	4
α-helix	862-868	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Catenin alpha-1	G, H, I, K, L, Z	protein	889	Homo sapiens	P35221 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>7UTJ_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (G, H, I, K, L, Z), FASTA

>7UTJ_2 Catenin alpha-1 (chains G, H, I, K, L, Z)
GPHMTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGD
KIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTR
LLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQE
LKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISN
AAQATASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAA
LMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRD
LRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLA
CSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRV
LTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVT
SEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRL
VYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLP
QEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLK
NTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVK
AEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAV
SWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6
MG	Magnesium ion	Mg	6

Primary citation

Distinct inter-domain interactions of dimeric versus monomeric alpha-catenin link cell junctions to filaments. Rangarajan, E.S., Smith, E.W., Izard, T. Commun Biol (2023) 6:276-276. DOI 10.1038/s42003-023-04610-x · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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