1FPR: Protein-tyrosine phosphatase 1C

Crystal structure of the complex formed between the catalytic domain of shp-1 and an in vitro peptide substrate PY469 derived from shps-1. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Mar 2001.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,374
Mol. weight: 33.79 kDa
Released: 7 Mar 2001

Explore 1FPR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FPR contains 9 α-helices and 22 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: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	246-253	8
β-strand	288-290	3	1
β-strand	303-305	3	1
β-strand	306	1	2
β-strand	307	1	1
β-strand	309-310	2	3
α-helix	316-318	3
β-strand	322-324	3	3
β-strand	326	1	2
β-strand	327	1	4
α-helix	331-333	3
α-helix	334-343	10
β-strand	348-351	4	3
β-strand	356	1	5
β-strand	363	1	5
β-strand	370	1	3
β-strand	372-376	5	3
β-strand	379-386	8	3
β-strand	392	1	6
β-strand	395-401	7	3
β-strand	409-413	5	3
β-strand	416	1	6
α-helix	429-442	14
β-strand	451-454	4	3
β-strand	457	1	4
α-helix	460-478	19
α-helix	483-484	2
α-helix	486-494	9
β-strand	495	1	7
β-strand	497	1	7
α-helix	505-525	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein-tyrosine phosphatase 1C	A	protein	284	Homo sapiens	P29350 (AlphaFold model)
Peptide PY469	B	protein	10

Sequence of entity 1 (A), FASTA

>1FPR_1 PROTEIN-TYROSINE PHOSPHATASE 1C (chains A)
GFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNILPFDHSRVILQGRDSNIPGSDYI
NANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCV
PYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGDLIREIWHYQYLSWPDHGV
PSEPGGVLSFLDQINQRQESLPHAGPIIVHSSAGIGRTGTIIVIDMLMENISTKGLDCDI
DIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEVL

Sequence of entity 2 (B), FASTA

>1FPR_2 PEPTIDE PY469 (chains B)
EDTLTYADLD

Primary citation

Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. Yang, J., Cheng, Z., Niu, T. et al. J Biol Chem (2000) 275:4066-4071. DOI 10.1074/jbc.275.6.4066 · PubMed

Other PDB entries of the same protein (UniProt P29350 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4GRZ 1.37 Å, Crystal structure of SHP1 catalytic domain with PO4
4HJP 1.4 Å, SHP-1 catalytic domain WPD loop open
4GRY 1.7 Å, Crystal structure of SHP1 catalytic domain with SO4
8YHI 1.75 Å, The Crystal Structure of SHP1 from Biortus.
4GS0 1.8 Å, Crystal structure of SHP1 catalytic domain with JAK1 activation loop peptide
4HJQ 1.8 Å, SHP-1 catalytic domain WPD loop closed
1GWZ 2.5 Å, Crystal structure of the catalytic domain of the protein tyrosine phosphatase shp-1
6SM5 2.75 Å, MbC/SHP1-C-SH2 complex
2B3O 2.8 Å, Crystal structure of human tyrosine phosphatase SHP-1
3PS5 3.1 Å, Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1
1X6C Solution structures of the SH2 domain of human protein-tyrosine phosphatase SHP-1
2RMX Solution structure of the SHP-1 C-terminal SH2 domain complexed with a…

Browse structure collections

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