6OBN: Coexpressed SDS22:PP1 complex

The crystal structure of coexpressed SDS22:PP1 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 18 Sept 2019.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,480
Mol. weight: 143.31 kDa
Ligands: PO4, FE
Released: 18 Sept 2019

Explore 6OBN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6OBN contains 29 α-helices and 60 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-17	15
α-helix	23	1
α-helix	32-47	16
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	135-143	9
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	229-238	10
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
β-strand	280-285	6	2
β-strand	291-296	6	2

Chain B: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-47	16
β-strand	52-55	4	5
β-strand	59-62	4	2
β-strand	64	1	6
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	135-143	9
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-171	3	5
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	7
β-strand	216-218	3	7
β-strand	225-227	3	7
α-helix	231-239	9
β-strand	243-246	4	5
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	267	1	6
β-strand	280-285	6	2
β-strand	291-296	6	2

Chains C and D: 4 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	80-82	3	8
α-helix	94-96	3
β-strand	102-104	3	8
β-strand	124-126	3	8
β-strand	146-148	3	8
β-strand	168-170	3	8
β-strand	190-192	3	8
β-strand	212-214	3	8
β-strand	234-236	3	8
β-strand	256-258	3	8
β-strand	278-280	3	8
β-strand	300-302	3	8
α-helix	311-317	7
β-strand	325-327	3	8
α-helix	332-335	4
α-helix	339-346	8
β-strand	352-353	2	8
β-strand	356-357	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, B	protein	305	Homo sapiens	P62136 (AlphaFold model)
Protein phosphatase 1 regulatory subunit 7	C, D	protein	310	Homo sapiens	Q15435 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6OBN_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, B)
GHMGSMSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLEL
EAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYP
ENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGG
LSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKF
LHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQI
LKPAD

Sequence of entity 2 (C, D), FASTA

>6OBN_2 Protein phosphatase 1 regulatory subunit 7 (chains C, D)
GHMGSEEDPEEEHELPVDMETINLDRDAEDVDLNHYRIGKIEGFEVLKKVKTLCLRQNLI
KCIENLEELQSLRELDLYDNQIKKIENLEALTELEILDISFNLLRNIEGVDKLTRLKKLF
LVNNKISKIENLSNLHQLQMLELGSNRIRAIENIDTLTNLESLFLGKNKITKLQNLDALT
NLTVLSMQSNRLTKIEGLQNLVNLRELYLSHNGIEVIEGLENNNKLTMLDIASNRIKKIE
NISHLTELQEFWMNDNLLESWSDLDELKGARSLETVYLERNPLQKDPQYRRKVMLALPSV
RQIDATFVRF

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	8
FE	FE (III) ion	Fe	2

Water and common crystallization additives (CL, MPD) are not listed.

Primary citation

SDS22 selectively recognizes and traps metal-deficient inactive PP1. Choy, M.S., Moon, T.M., Ravindran, R. et al. Proc Natl Acad Sci U S A (2019) 116:20472-20481. DOI 10.1073/pnas.1908718116 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZEG 1.09 Å, Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to…
6ZEH 1.3 Å, Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha…
6ZEI 1.39 Å, Structure of PP1-IRSp53 S455E chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)]…
6DNO 1.45 Å, Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting…
4MOV 1.45 Å, 1.45 A Resolution Crystal Structure of Protein Phosphatase 1
6OBR 1.5 Å, PP1 Y134A in complex with Microcystin LR
3E7A 1.63 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin Nodularin-R
3E7B 1.7 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin
8SW6 1.76 Å, Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide…
6ZEJ 1.78 Å, Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
7T0Y 1.8 Å, The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme
6OBS 1.8 Å, PP1 Y134K

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