4QUM: PTPN3

Crystal structure of PTPN3 (PTPH1) in complex with a dually phosphorylated MAPK12 peptide. Determined by X-ray diffraction at 2.52 Å resolution. Released 10 Dec 2014.

Method: X-ray diffraction
Resolution: 2.52 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,339
Mol. weight: 36.13 kDa
Released: 10 Dec 2014

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

Secondary structure: helices and β-sheets

4QUM contains 15 α-helices and 11 β-strands across 1 chain. 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: 15 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	630-643	14
α-helix	645-652	8
α-helix	664-666	3
α-helix	671-673	3
β-strand	686-688	3	1
α-helix	689	1
β-strand	695-705	11	1
α-helix	706-708	3
β-strand	710-717	8	1
α-helix	718-721	4
α-helix	725-734	10
β-strand	739-742	4	1
β-strand	747-748	2	2
β-strand	751-752	2	2
α-helix	759-760	2
β-strand	764-766	3	1
β-strand	770-779	10	1
β-strand	783-792	10	1
β-strand	798-806	9	1
α-helix	818-831	14
α-helix	832-833	2
α-helix	837	1
β-strand	838-841	4	1
α-helix	847-863	17
α-helix	870-878	9
α-helix	888-904	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein phosphatase non-receptor type 3	A	protein	306	Homo sapiens	P26045 (AlphaFold model)
Mitogen-activated protein kinase 12	B	protein	9	Homo sapiens	P53778 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4QUM_1 Tyrosine-protein phosphatase non-receptor type 3 (chains A)
MHHHHHHSSGVDLGTENLYFQSNADTLEGSMAQLKKGLESGTVLIQFEQLYRKKPGLAIT
FAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPH
TCAQFWQVVWDQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMNHGGFHIQCQSEDCTIAY
VSREMLVTNTQTGEEHTVTHLQYVAWPAHGVPDDSSDFLEFVNYVRSLRVDSEPVLVHSS
AGIGRTGVLVTMETAMCLTERNLPIYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYE
EGLVQM

Sequence of entity 2 (B), FASTA

>4QUM_2 Mitogen-activated protein kinase 12 (chains B)
MTGYVVTRR

Primary citation

Reciprocal allosteric regulation of p38 gamma and PTPN3 involves a PDZ domain-modulated complex formation. Chen, K.E., Lin, S.Y., Wu, M.J. et al. Sci Signal (2014) 7:ra98-ra98. DOI 10.1126/scisignal.2005722 · PubMed

Other PDB entries of the same protein (UniProt P26045 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4RI5 1.26 Å, Crystal structure of PTPN3 (PTPH1) D811E mutant in complex with metavanadate
2B49 1.54 Å, Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase, non-receptor…
4RHG 1.58 Å, Crystal structure of PTPN3 (PTPH1) D811E, C842S mutant in complex with Eps15 pTyr849…
4RI4 1.6 Å, Crystal structure of PTPN3 (PTPH1) Y676I mutant in complex with vanadate
4RH9 1.6 Å, Crystal structure of PTPN3 (PTPH1) H812F, M883G mutant in complex with Eps15 pTyr849…
4RH5 1.6 Å, Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 peptide
8CQY 1.7 Å, Crystal structure of the PTPN3 PDZ domain bound to the PBM TACE C-terminal peptide
4S0G 1.72 Å, Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 P850V peptide
4QUN 1.86 Å, Crystal structure of the PTPN3 (PTPH1) catalytic domain C842S mutant
6T36 1.86 Å, Crystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptide
8OEP 1.87 Å, Crystal structure of the PTPN3 PDZ domain bound to the HPV18 E6 oncoprotein C-terminal…
6HKS 2.19 Å, Crystal structure of the PTPN3 PDZ domain bound to the HPV16 E6 oncoprotein C-terminal…

Browse structure collections

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