4V0U: Ternary PP1G-PPP1R15B and G-actin complex

The crystal structure of ternary PP1G-PPP1R15B and G-actin complex. Determined by X-ray diffraction at 7.88 Å resolution. Released 25 Mar 2015.

Method: X-ray diffraction
Resolution: 7.88 Å
Organisms: ORYCTOLAGUS CUNICULUS, MUS MUSCULUS, HOMO SAPIENS
Chains: 15
Atoms: 27,065
Mol. weight: 450.46 kDa
Ligands: LAB, ATP, MN
Released: 25 Mar 2015

Explore 4V0U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V0U contains 180 α-helices and 197 β-strands across 15 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, B and C: 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	53-54	2	2
α-helix	55-60	6
α-helix	62-64	3
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	89-93	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	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	246	1	6
β-strand	247-250	4	5
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-373	5

Chain D: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	17
β-strand	59-62	4	18
β-strand	64	1	19
α-helix	69-79	11
β-strand	87-89	3	18
α-helix	100-113	14
β-strand	118-120	3	18
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	17
β-strand	169-172	4	17
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	20
β-strand	216-218	3	20
β-strand	225-227	3	20
α-helix	229-239	11
β-strand	243-246	4	17
β-strand	255-258	4	17
β-strand	263-266	4	17
β-strand	267	1	19
α-helix	272-274	3
β-strand	280-285	6	18
β-strand	290-299	10	18

Chains E, G, I, K and O: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	642-643	2	18
β-strand	648-653	6	18

Chains F, H and N: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	21
β-strand	59-62	4	22
β-strand	64	1	23
α-helix	69-79	11
β-strand	87-89	3	22
α-helix	100-113	14
β-strand	118-120	3	22
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	21
β-strand	169-172	4	21
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	24
β-strand	213	1	25
β-strand	216-218	3	24
β-strand	225-227	3	24
α-helix	229-239	11
β-strand	243-246	4	21
β-strand	255-258	4	21
β-strand	263-266	4	21
β-strand	267	1	23
α-helix	272-274	3
β-strand	276	1	26
β-strand	280-285	6	22
β-strand	290-299	10	22

Chain J: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	31
β-strand	59-62	4	32
β-strand	64	1	33
α-helix	69-79	11
β-strand	87-89	3	32
α-helix	100-113	14
β-strand	118-120	3	32
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	31
β-strand	169-172	4	31
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	34
β-strand	213	1	35
β-strand	216-218	3	34
β-strand	225-227	3	34
α-helix	229-239	11
β-strand	243-246	4	31
β-strand	255-258	4	31
β-strand	263-266	4	31
β-strand	267	1	33
α-helix	272-274	3
β-strand	276	1	36
β-strand	280-285	6	32
β-strand	290-299	10	32

Chain L: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	37
β-strand	16-21	6	37
β-strand	29-32	4	37
β-strand	35-38	4	38
β-strand	53-54	2	38
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	38
β-strand	71-72	2	39
β-strand	75-76	2	39
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	37
α-helix	113-125	13
β-strand	131-136	6	37
α-helix	137-144	8
β-strand	150-155	6	40
β-strand	160-166	7	40
β-strand	169-170	2	40
α-helix	172-174	3
β-strand	176-178	3	40
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	41
β-strand	247-250	4	41
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	40
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	40
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	37
α-helix	359-365	7
α-helix	369-373	5

Chain M: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-38	4	42
β-strand	53-54	2	42
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	42
β-strand	71-72	2	43
β-strand	75-76	2	43
α-helix	79-88	10
α-helix	89-93	5
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	44
β-strand	160-166	7	44
β-strand	169-170	2	44
α-helix	172-174	3
β-strand	176-178	3	44
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	45
β-strand	246	1	11
β-strand	247-250	4	45
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	44
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	44
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	369-373	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, L, M	protein	375	ORYCTOLAGUS CUNICULUS	P68135 (AlphaFold model)
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit	D, F, H, J, N	protein	323	MUS MUSCULUS	P63087 (AlphaFold model)
Protein phosphatase 1 regulatory subunit 15B	E, G, I, K, O	protein	84	HOMO SAPIENS	Q5SWA1 (AlphaFold model)

Sequence of entity 1 (A, B, C, L, M), FASTA

>4V0U_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B, C, L, M)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (D, F, H, J, N), FASTA

>4V0U_2 SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT (chains D, F, H, J, N)
MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK

Sequence of entity 3 (E, G, I, K, O), FASTA

>4V0U_3 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B (chains E, G, I, K, O)
GAMDPGRHTHVKRKKVTFLEEVTEYYISGDEDRKGPWEEFARDGCRFQKRIQETEDAIGY
CLTFEHRERMFNRLQGLEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
LAB	Latrunculin B	C20 H29 N O5 S	5
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	5
MN	Manganese (II) ion	Mn	10

Primary citation

G-actin provides substrate-specificity to eukaryotic initiation factor 2 alpha holophosphatases. Chen, R., Rato, C., Yan, Y. et al. Elife (2015) 4. DOI 10.7554/eLife.04871 · 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

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