4V0V: Mouse PP1G

The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660). Determined by X-ray diffraction at 1.61 Å resolution. Released 25 Mar 2015.

Method: X-ray diffraction
Resolution: 1.61 Å
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 4
Atoms: 5,493
Mol. weight: 76.12 kDa
Ligands: MN
Released: 25 Mar 2015

Explore 4V0V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V0V contains 25 α-helices and 36 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: 12 helices, 16 β-strands

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

Chain B: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	642-643	2	2
α-helix	646-647	2
β-strand	648-653	6	2

Chain C: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	17-20	4
α-helix	32-48	17
β-strand	52-55	4	5
β-strand	59-62	4	6
β-strand	64	1	7
α-helix	69-79	11
β-strand	87-89	3	6
α-helix	100-113	14
β-strand	118-120	3	6
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	184-187	4
α-helix	200-206	7
β-strand	208-209	2	8
β-strand	216-218	3	8
β-strand	225-227	3	8
α-helix	229-239	11
β-strand	243-246	4	5
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	267	1	7
α-helix	272-274	3
β-strand	280-285	6	6
β-strand	290-298	9	6

Chain D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	642-643	2	6
β-strand	648-652	5	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit	A, C	protein	295	MUS MUSCULUS	P63087 (AlphaFold model)
Protein phosphatase 1 regulatory subunit 15B	B, D	protein	35	HOMO SAPIENS	Q5SWA1 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4V0V_1 SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT (chains A, C)
MLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDI
HGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNH
ECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQ
IRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLIC
RAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE

Sequence of entity 2 (B, D), FASTA

>4V0V_2 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B (chains B, D)
GAMDPGRHTHVKRKKVTFLEEVTEYYISGDEDRKG

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	2

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

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 P63087 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4V0W 1.55 Å, The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)
4V0X 1.85 Å, The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)
9IJJ 7.7 Å, In situ structure of the central apparatus in mouse sperm axoneme.
4V0U 7.88 Å, The crystal structure of ternary PP1G-PPP1R15B and G-actin complex

Browse structure collections

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