1HLU: Beta-actin

Structure of bovine beta-actin-profilin complex with actin bound ATP phosphates solvent accessible. Determined by X-ray diffraction at 2.65 Å resolution. Released 15 Oct 1997.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Bos taurus
Chains: 2
Atoms: 4,000
Mol. weight: 57.21 kDa
Ligands: ATP, CA
Released: 15 Oct 1997

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

Secondary structure: helices and β-sheets

1HLU contains 28 α-helices and 27 β-strands across 2 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.

Chain A: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	30-32	3	1
β-strand	35-38	4	2
β-strand	53-54	2	2
α-helix	57-61	5
β-strand	63	1	2
β-strand	65-68	4	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	182-193	12
α-helix	194-196	3
α-helix	206-216	11
α-helix	223-231	9
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	252-256	5
α-helix	258-260	3
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-293	7
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-318	10
β-strand	330	1	4
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-373	5

Chain P: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-11	8
β-strand	16-23	8	6
β-strand	29-33	5	6
α-helix	39-41	3
α-helix	44-50	7
α-helix	57-60	4
β-strand	63-64	2	6
β-strand	69-75	7	6
β-strand	84-89	6	6
β-strand	99-104	6	6
β-strand	108-114	7	6
α-helix	120-136	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-actin	A	protein	375	Bos taurus	P60712 (AlphaFold model)
Profilin	P	protein	140	Bos taurus	P02584 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1HLU_1 BETA-ACTIN (chains A)
XDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Sequence of entity 2 (P), FASTA

>1HLU_2 PROFILIN (chains P)
XAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGILVGKDRSSFF
VNGLTLGGQKCSVIRDSLLQDGEFTMDLRTKSTGGAPTFNITVTMTAKTLVLLMGKEGVH
GGMINKKCYEMASHLRRSQY

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
CA	Calcium ion	Ca	1

Primary citation

The structure of an open state of beta-actin at 2.65 A resolution. Chik, J.K., Lindberg, U., Schutt, C.E. J Mol Biol (1996) 263:607-623. DOI 10.1006/jmbi.1996.0602 · PubMed

Other PDB entries of the same protein (UniProt P60712 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3UB5 2.2 Å, Profilin:actin with a wide open nucleotide cleft
3U4L 2.4 Å, Cryocooled bovine profilin:actin crystal structure to 2.4 A
2BTF 2.55 Å, The structure of crystalline profilin-beta-actin
2OAN 2.61 Å, Structure of oxidized beta-actin
8OI6 3.59 Å, Cryo-EM structure of the undecorated barbed end of filamentous beta/gamma actin
9FJY 3.79 Å, Structure of the DNase I- and phalloidin-bound pointed end of F-actin (conformer 2).
7PDZ 3.8 Å, Structure of capping protein bound to the barbed end of a cytoplasmic actin filament
9FJU 3.84 Å, Structure of the DNase I- and phalloidin-bound pointed end of F-actin (conformer 1)

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