4YFE: PTP delta Fn1-Fn2

Crystal structure of PTP delta Fn1-Fn2. Determined by X-ray diffraction at 1.97 Å resolution. Released 6 May 2015.

Method: X-ray diffraction
Resolution: 1.97 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,296
Mol. weight: 44.35 kDa
Released: 6 May 2015

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

Secondary structure: helices and β-sheets

4YFE contains 17 α-helices and 32 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: 9 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	329-336	8
β-strand	337-341	5	1
β-strand	346-349	4	1
α-helix	357-358	2
β-strand	360-367	8	2
α-helix	373-374	2
β-strand	375-380	6	2
β-strand	384-387	4	1
β-strand	395-403	9	2
β-strand	408-411	4	2
α-helix	412-414	3
β-strand	415-418	4	2
α-helix	419-421	3
α-helix	427-428	2
β-strand	429-435	7	3
β-strand	441-446	6	3
β-strand	457-463	7	4
α-helix	470-472	3
β-strand	474-479	6	4
β-strand	483-486	4	3
α-helix	489-490	2
β-strand	494-502	9	4
β-strand	507	1	4
α-helix	509-513	5
β-strand	514-517	4	4

Chain B: 8 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	329-336	8
β-strand	337-341	5	5
β-strand	346-349	4	5
α-helix	357-358	2
β-strand	360-367	8	6
α-helix	373-374	2
β-strand	375-380	6	6
β-strand	384-387	4	5
β-strand	395-403	9	6
β-strand	408-411	4	6
β-strand	415-418	4	6
α-helix	419-421	3
α-helix	427-428	2
β-strand	429-435	7	7
β-strand	441-446	6	7
β-strand	457-463	7	8
α-helix	470-472	3
β-strand	474-479	6	8
β-strand	483-486	4	7
α-helix	489-490	2
β-strand	494-502	9	8
β-strand	507-510	4	8
α-helix	511-513	3
β-strand	514-517	4	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Receptor-type tyrosine-protein phosphatase delta	A, B	protein	200	Mus musculus	Q64487 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4YFE_1 Receptor-type tyrosine-protein phosphatase delta (chains A, B)
MALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYS
VAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQTSEQAPSSAPRDVQARMLSSTTILVQWK
EPEEPNGQIQGYRVYYTMDPTQHVNNWMKHNVADSQITTIGNLVPQKTYSVKVLAFTSIG
DGPLSSDIQVITLEHHHHHH

Primary citation

Mechanisms of splicing-dependent trans-synaptic adhesion by PTP delta-IL1RAPL1/IL-1RAcP for synaptic differentiation. Yamagata, A., Yoshida, T., Sato, Y. et al. Nat Commun (2015) 6:6926-6926. DOI 10.1038/ncomms7926 · PubMed

Other PDB entries of the same protein (UniProt Q64487 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KIP 1.91 Å, Crystal structure of PTPRD phosphatase domain in complex with Liprin-alpha3 tandem SAM…
5Y32 2.7 Å, Crystal structure of PTP delta Ig1-Ig2 in complex with IL1RAPL1
5XWU 3.16 Å, Crystal structure of PTPdelta Ig1-Ig3 in complex with SALM2 LRR-Ig
4YFD 3.25 Å, Crystal structure PTP delta Ig1-Fn2 in complex with IL-1RAcP
4Y61 3.36 Å, Crystal structure of the complex between Slitrk2 LRR1 and PTP delta Ig1-Fn1
4YFG 3.49 Å, Crystal structure of PTP delta meA3/meB minus variant Ig1-Fn1
7CEG 3.85 Å, Crystal structure of the complex between mouse PTP delta and neuroligin-3
5XWT 4.18 Å, Crystal structure of PTPdelta Ig1-Fn1 in complex with SALM5 LRR-Ig
4YH7 4.4 Å, Crystal structure of PTPdelta ectodomain in complex with IL1RAPL1

Browse structure collections

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