2OAN: Oxidized beta-actin

Structure of oxidized beta-actin. Determined by X-ray diffraction at 2.61 Å resolution. Released 1 May 2007.

Method: X-ray diffraction
Resolution: 2.61 Å
Organism: Bos taurus
Chains: 4
Atoms: 11,679
Mol. weight: 169.93 kDa
Ligands: ATP, CA
Released: 1 May 2007

Explore 2OAN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OAN contains 90 α-helices and 76 β-strands across 4 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: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-37	3	2
β-strand	53-54	2	2
α-helix	56-59	4
α-helix	62-64	3
β-strand	66-68	3	2
β-strand	71	1	3
β-strand	76	1	3
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
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	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-259	7
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-369	4

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-11	4	6
β-strand	16-21	6	6
β-strand	29-32	4	6
β-strand	35-38	4	7
β-strand	53-54	2	7
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	7
β-strand	71	1	8
β-strand	76	1	8
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	6
α-helix	137-144	8
β-strand	150-155	6	9
β-strand	160-166	7	9
β-strand	169-170	2	9
α-helix	172-174	3
β-strand	176-178	3	9
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	9
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-347	10
α-helix	352-355	4
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	367-372	6

Chain C: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-37	3	12
β-strand	53-54	2	12
α-helix	56-59	4
α-helix	62-64	3
β-strand	66-68	3	12
β-strand	71	1	13
β-strand	76	1	13
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	11
α-helix	137-144	8
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
α-helix	172-174	3
β-strand	176-178	3	14
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	14
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	11
α-helix	359-363	5
α-helix	367-369	3

Chain D: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-37	3	17
β-strand	53-54	2	17
α-helix	56-59	4
α-helix	62-64	3
β-strand	66-68	3	17
β-strand	71	1	18
β-strand	76	1	18
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-144	8
β-strand	150-155	6	19
β-strand	160-166	7	19
β-strand	169-170	2	19
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	19
α-helix	302-304	3
α-helix	309-320	12
α-helix	325-327	3
β-strand	329-330	2	19
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	367-372	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, cytoplasmic 1	A, B, C, D	protein	375	Bos taurus	P60712 (AlphaFold model)

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

>2OAN_1 Actin, cytoplasmic 1 (chains A, B, C, D)
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	4
CA	Calcium ion	Ca	4

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

Primary citation

Molecular and Structural Basis for Redox Regulation of beta-Actin. Lassing, I., Schmitzberger, F., Bjornstedt, M. et al. J Mol Biol (2007) 370:331-348. DOI 10.1016/j.jmb.2007.04.056 · 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
1HLU 2.65 Å, Structure of bovine beta-actin-profilin complex with actin bound ATP phosphates solvent…
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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