4JMG: Synthetic protein

Crystal structure of the synthetic protein in complex with pY peptide. Determined by X-ray diffraction at 1.4 Å resolution. Released 23 Apr 2014.

Method: X-ray diffraction
Resolution: 1.4 Å
Organisms: synthetic construct, Homo sapiens
Chains: 2
Atoms: 1,776
Mol. weight: 23.77 kDa
Ligands: MG
Released: 23 Apr 2014

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

Secondary structure: helices and β-sheets

4JMG contains 5 α-helices and 18 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: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
α-helix	8-14	7
β-strand	29-30	2	2
β-strand	41	1	2
α-helix	47-55	9
β-strand	62-67	6	2
β-strand	75-81	7	2
β-strand	84-89	6	2
α-helix	90	1
β-strand	91-92	2	1
β-strand	98-99	2	1
β-strand	117-121	5	3
β-strand	126-129	4	3
β-strand	142-149	8	4
α-helix	155-156	2
β-strand	157-162	6	4
β-strand	167-170	4	3
α-helix	173-174	2
β-strand	178-185	8	4
β-strand	186	1	5
β-strand	191-193	3	5
β-strand	197-202	6	4

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	583-585	3	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Clamp Ptpn11_pY580	A	protein	203	synthetic construct
Tyrosine-protein phosphatase non-receptor type 11	B	protein	13	Homo sapiens	Q06124 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4JMG_1 Clamp Ptpn11_pY580 (chains A)
GSVKFNSLNELVDYHRSTSVSRNQQIFLRDIGGSGGGHPWYKGKIPRAKAEEMLSKQRHD
GAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVGGSGGSVSSVPTKLEVVA
ATPTSLLISWDAWSGSDWPVSYYRITYGETGGNSPVQEFTVPGSSYTATISGLSPGVDYT
ITVYAGYDGKYYYQSPISINYRT

Sequence of entity 2 (B), FASTA

>4JMG_2 Tyrosine-protein phosphatase non-receptor type 11 (chains B)
DSARVYENVGLMQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Primary citation

Directed network wiring identifies a key protein interaction in embryonic stem cell differentiation. Yasui, N., Findlay, G.M., Gish, G.D. et al. Mol Cell (2014) 54:1034-1041. DOI 10.1016/j.molcel.2014.05.002 · PubMed

Other PDB entries of the same protein (UniProt Q06124 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9EIK 1.25 Å, Crystal structure of N-SH2 domain of SHP2 with T42A mutation bound to GAB1 tyrosine…
3ZM1 1.4 Å, Catalytic domain of human SHP2
7PPM 1.48 Å, SHP2 catalytic domain in complex with IRS1 (889-901) phosphopeptide (pSer-892, pTyr-896)
3ZM0 1.5 Å, Catalytic domain of human SHP2
3ZM2 1.5 Å, Catalytic domain of human SHP2
3ZM3 1.5 Å, Catalytic domain of human SHP2
7PPL 1.53 Å, SHP2 catalytic domain in complex with IRS1 (625-639) phosphopeptide (pTyr-632, pSer-636)
9EIC 1.58 Å, Crystal structure of unbound N-SH2 domain of SHP2 with T42A mutation
9EHD 1.59 Å, Crystal structure of N-SH2 domain of SHP2 bound to GAB1 tyrosine phosphorylated peptide…
3B7O 1.6 Å, Crystal structure of the human tyrosine phosphatase SHP2 (PTPN11) with an accessible…
4RDD 1.6 Å, Co-crystal structure of SHP2 in complex with a Cefsulodin derivative
5EHR 1.7 Å, Non-receptor Protein Tyrosine Phosphatase SHP2 in Complex with Allosteric Inhibitor SHP099

Browse structure collections

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