4HJQ: SHP-1 catalytic domain WPD loop closed

SHP-1 catalytic domain WPD loop closed. Determined by X-ray diffraction at 1.8 Å resolution. Released 3 Apr 2013.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,334
Mol. weight: 70.93 kDa
Ligands: PO4
Released: 3 Apr 2013

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

Secondary structure: helices and β-sheets

4HJQ contains 28 α-helices and 22 β-strands across 2 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: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	244-255	12
α-helix	263-266	4
α-helix	268-273	6
α-helix	283-285	3
β-strand	286-288	3	1
α-helix	289-290	2
β-strand	301-307	7	1
β-strand	321-324	4	1
α-helix	325-328	4
α-helix	329-331	3
α-helix	332-341	10
β-strand	346-349	4	1
β-strand	354-355	2	2
β-strand	358-359	2	2
α-helix	366-367	2
β-strand	371-374	4	1
β-strand	377-386	10	1
β-strand	390-399	10	1
β-strand	407-414	8	1
α-helix	427-441	15
α-helix	448	1
β-strand	449-452	4	1
α-helix	459-476	18
α-helix	484-492	9
α-helix	502-522	21

Chain B: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	244-256	13
α-helix	268-273	6
α-helix	283-285	3
β-strand	286	1	3
α-helix	287-289	3
β-strand	304-308	5	3
α-helix	314-316	3
β-strand	320-324	5	3
α-helix	325-328	4
α-helix	329-331	3
α-helix	332-341	10
β-strand	346-349	4	3
β-strand	354-355	2	4
β-strand	358-359	2	4
α-helix	366-367	2
β-strand	371-374	4	3
β-strand	377-386	10	3
β-strand	390-399	10	3
β-strand	407-414	8	3
α-helix	427-442	16
α-helix	448	1
β-strand	449-452	4	3
α-helix	458-476	19
α-helix	484-492	9
α-helix	502-521	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein phosphatase non-receptor type 6	A, B	protein	308	Homo sapiens	P29350 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4HJQ_1 Tyrosine-protein phosphatase non-receptor type 6 (chains A, B)
MHHHHHHGSLVPRSENLYFQGSGFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNIL
PFDHSRVILQGRDSNIPGSDYINANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAW
QENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPL
DNGDLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHSSAGIGRT
GTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTK
KKLEVLQS

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

Primary citation

SHP Family Protein Tyrosine Phosphatases Adopt Canonical Active-Site Conformations in the Apo and Phosphate-Bound States. Alicea-Velazquez, N.L., Boggon, T.J. Protein Pept Lett (2013) 20:1039-1048. 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
1FPR 2.5 Å, Crystal structure of the complex formed between the catalytic domain of shp-1 and an in…
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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