2HV7: Phosphotyrosyl phosphatase activator

Crystal structure of phosphotyrosyl phosphatase activator bound to ATPgammaS. Determined by X-ray diffraction at 2.5 Å resolution. Released 22 Aug 2006.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 19,612
Mol. weight: 296.26 kDa
Ligands: ADP
Released: 22 Aug 2006

Explore 2HV7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HV7 contains 188 α-helices and 56 β-strands across 8 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: 24 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	1
α-helix	33-35	3
α-helix	36-40	5
β-strand	42	1	2
α-helix	43-59	17
α-helix	72-90	19
α-helix	92-94	3
α-helix	104-120	17
α-helix	126-128	3
α-helix	131-140	10
β-strand	145	1	3
β-strand	150-151	2	3
α-helix	153-168	16
α-helix	174-176	3
α-helix	179	1
α-helix	180-185	6
α-helix	186-198	13
α-helix	201	1
β-strand	202-203	2	3
α-helix	205-208	4
α-helix	218-226	9
α-helix	235-239	5
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-278	6
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	1
β-strand	319	1	2

Chain B: 21 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	4
α-helix	33-40	8
β-strand	42	1	5
α-helix	43-58	16
α-helix	72-89	18
α-helix	92-95	4
α-helix	104-121	18
α-helix	132-140	9
β-strand	145	1	6
β-strand	150-151	2	6
α-helix	153-168	16
α-helix	174-176	3
α-helix	177-179	3
α-helix	180-185	6
α-helix	186-199	14
α-helix	201	1
β-strand	202-203	2	6
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-278	6
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	4
β-strand	319	1	5

Chain C: 22 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	7
α-helix	33-41	9
β-strand	42	1	8
α-helix	43-58	16
α-helix	72-90	19
α-helix	92-95	4
α-helix	105-120	16
α-helix	126-131	6
α-helix	132-140	9
β-strand	145	1	9
β-strand	150-151	2	9
α-helix	153-168	16
α-helix	174-176	3
α-helix	177-179	3
α-helix	180-185	6
α-helix	186-199	14
α-helix	201	1
β-strand	202-203	2	9
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-278	6
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	7
β-strand	319	1	8

Chain D: 26 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	10
α-helix	33-35	3
α-helix	36-40	5
β-strand	42	1	11
α-helix	43-59	17
α-helix	72-90	19
α-helix	92-94	3
α-helix	104-120	17
α-helix	126-131	6
α-helix	132-140	9
β-strand	145	1	12
β-strand	150-151	2	12
α-helix	153-168	16
α-helix	174-176	3
α-helix	179	1
α-helix	180-185	6
α-helix	186-198	13
α-helix	201	1
β-strand	202-203	2	12
α-helix	205-207	3
α-helix	218-226	9
α-helix	235-239	5
α-helix	241-247	7
α-helix	248-250	3
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-279	7
α-helix	284-294	11
α-helix	295-300	6
α-helix	303-306	4
β-strand	310-311	2	10
β-strand	319	1	11
α-helix	320	1

Chain E: 24 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	13
α-helix	33-41	9
β-strand	42	1	14
α-helix	43-58	16
α-helix	72-89	18
α-helix	92-95	4
α-helix	104-114	11
α-helix	116-120	5
α-helix	126-131	6
α-helix	132-140	9
β-strand	145	1	15
β-strand	150-151	2	15
α-helix	153-164	12
α-helix	165-167	3
α-helix	174-176	3
α-helix	177-179	3
α-helix	180-185	6
α-helix	186-199	14
α-helix	201	1
β-strand	202-203	2	15
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-278	6
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	13
β-strand	319	1	14

Chain F: 25 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	16
α-helix	33-35	3
α-helix	36-40	5
β-strand	42	1	17
α-helix	43-59	17
α-helix	72-90	19
α-helix	92-94	3
α-helix	104-120	17
α-helix	126-131	6
α-helix	132-140	9
β-strand	145	1	18
β-strand	150-151	2	18
α-helix	153-168	16
α-helix	174-177	4
α-helix	179	1
α-helix	180-185	6
α-helix	186-198	13
α-helix	201	1
β-strand	202-203	2	18
α-helix	207-210	4
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-279	7
α-helix	284-294	11
α-helix	295-300	6
α-helix	303-306	4
β-strand	310-311	2	16
β-strand	319	1	17
α-helix	320	1

Chain G: 22 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	19
α-helix	33-41	9
β-strand	42	1	20
α-helix	43-57	15
α-helix	74-90	17
α-helix	92-95	4
α-helix	104-121	18
α-helix	126-128	3
α-helix	132-140	9
β-strand	145	1	21
β-strand	150-151	2	21
α-helix	153-168	16
α-helix	174-176	3
α-helix	177-179	3
α-helix	180-185	6
α-helix	186-199	14
α-helix	201	1
β-strand	202-203	2	21
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-245	5
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-279	7
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	19
β-strand	319	1	20

Chain H: 24 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	22
α-helix	33-35	3
α-helix	36-40	5
β-strand	42	1	23
α-helix	43-59	17
α-helix	72-90	19
α-helix	92-94	3
α-helix	104-120	17
α-helix	126-131	6
α-helix	132-140	9
β-strand	145	1	24
β-strand	150-151	2	24
α-helix	153-168	16
α-helix	174-176	3
α-helix	179	1
α-helix	180-185	6
α-helix	186-198	13
α-helix	201	1
β-strand	202-203	2	24
α-helix	205-208	4
α-helix	218-226	9
α-helix	235-237	3
α-helix	241-247	7
α-helix	252-263	12
α-helix	268-271	4
α-helix	273-280	8
α-helix	284-295	12
α-helix	296-300	5
α-helix	303-306	4
β-strand	310-311	2	22
β-strand	319	1	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein phosphatase 2A, regulatory subunit B	A, B, C, D, E, F, G, H	protein	323	Homo sapiens	Q15257 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>2HV7_1 Protein phosphatase 2A, regulatory subunit B (chains A, B, C, D, E, F, G, H)
MAEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVK
GKKLTFEYRVSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLV
ATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAI
VFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVD
EKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECL
EKFPVIQHFKFGSLLPIHPVTSG

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4

Primary citation

Structure and mechanism of the phosphotyrosyl phosphatase activator. Chao, Y., Xing, Y., Chen, Y. et al. Mol Cell (2006) 23:535-546. DOI 10.1016/j.molcel.2006.07.027 · PubMed

Other PDB entries of the same protein (UniProt Q15257 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IXM 1.5 Å, Structure of human PTPA
2G62 1.6 Å, Crystal structure of human PTPA
4NY3 1.8 Å, Human PTPA in complex with peptide
2HV6 1.9 Å, Crystal structure of the phosphotyrosyl phosphatase activator
4LAC 2.82 Å, Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A phosphatase activator (PTPA)…

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