Crystal structure of PTPdelta Ig1-Ig3 in complex with SALM2 LRR-Ig. Determined by X-ray diffraction at 3.16 Å resolution. Released 6 Jun 2018.
Explore 5XWU in 3D Show helices and sheets RCSB PDB PDBe
5XWU contains 41 α-helices and 113 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 2 |
| β-strand | 48-57 | 10 | 1 |
| α-helix | 59-60 | 2 | |
| β-strand | 61-66 | 6 | 3 |
| β-strand | 69-70 | 2 | 3 |
| α-helix | 71 | 1 | |
| β-strand | 76-80 | 5 | 1 |
| β-strand | 86-91 | 6 | 1 |
| β-strand | 102-108 | 7 | 3 |
| β-strand | 113-119 | 7 | 3 |
| β-strand | 120-123 | 4 | 2 |
| α-helix | 125-127 | 3 | |
| β-strand | 134-137 | 4 | 4 |
| β-strand | 142-145 | 4 | 2 |
| β-strand | 150-152 | 3 | 5 |
| β-strand | 155-157 | 3 | 4 |
| α-helix | 161-162 | 2 | |
| β-strand | 163-168 | 6 | 2 |
| β-strand | 171-172 | 2 | 2 |
| β-strand | 182-184 | 3 | 5 |
| β-strand | 199-201 | 3 | 5 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-217 | 8 | 2 |
| β-strand | 222-224 | 3 | 2 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-233 | 6 | 2 |
| α-helix | 234-235 | 2 | |
| β-strand | 241-247 | 7 | 6 |
| α-helix | 248-251 | 4 | |
| β-strand | 252-254 | 3 | 7 |
| β-strand | 259-269 | 11 | 6 |
| α-helix | 271-272 | 2 | |
| β-strand | 273-278 | 6 | 7 |
| β-strand | 281-282 | 2 | 7 |
| β-strand | 291 | 1 | 7 |
| β-strand | 293-299 | 7 | 6 |
| β-strand | 305-313 | 9 | 7 |
| β-strand | 316-326 | 11 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-35 | 2 | |
| β-strand | 39-41 | 3 | 8 |
| β-strand | 48-50 | 3 | 8 |
| α-helix | 59-60 | 2 | |
| β-strand | 69-71 | 3 | 8 |
| β-strand | 79-80 | 2 | 9 |
| β-strand | 93-95 | 3 | 8 |
| β-strand | 103-104 | 2 | 9 |
| β-strand | 117-119 | 3 | 8 |
| β-strand | 127-128 | 2 | 10 |
| β-strand | 141-143 | 3 | 8 |
| β-strand | 151-152 | 2 | 10 |
| α-helix | 153 | 1 | |
| α-helix | 158-160 | 3 | |
| β-strand | 166-168 | 3 | 8 |
| α-helix | 179-182 | 4 | |
| β-strand | 190-192 | 3 | 8 |
| β-strand | 214-216 | 3 | 8 |
| β-strand | 246-248 | 3 | 8 |
| β-strand | 254-255 | 2 | 11 |
| α-helix | 258-260 | 3 | |
| α-helix | 261-264 | 4 | |
| β-strand | 274 | 1 | 12 |
| β-strand | 275-277 | 3 | 11 |
| α-helix | 279-281 | 3 | |
| β-strand | 285 | 1 | 12 |
| α-helix | 286-288 | 3 | |
| α-helix | 291-293 | 3 | |
| β-strand | 297-303 | 7 | 13 |
| β-strand | 317-319 | 3 | 14 |
| β-strand | 322-326 | 5 | 13 |
| α-helix | 328-329 | 2 | |
| β-strand | 330-334 | 5 | 15 |
| β-strand | 340-341 | 2 | 15 |
| β-strand | 347-349 | 3 | 14 |
| β-strand | 355-357 | 3 | 14 |
| β-strand | 367-374 | 8 | 15 |
| β-strand | 377-384 | 8 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-35 | 7 | 16 |
| β-strand | 40-43 | 4 | 17 |
| β-strand | 48-57 | 10 | 16 |
| α-helix | 59-60 | 2 | |
| β-strand | 61-66 | 6 | 18 |
| β-strand | 69-70 | 2 | 18 |
| α-helix | 71 | 1 | |
| β-strand | 76-80 | 5 | 16 |
| β-strand | 86-91 | 6 | 16 |
| β-strand | 102-108 | 7 | 18 |
| β-strand | 113-119 | 7 | 18 |
| β-strand | 120-123 | 4 | 17 |
| α-helix | 125-127 | 3 | |
| α-helix | 128-129 | 2 | |
| β-strand | 134-137 | 4 | 19 |
| β-strand | 142-145 | 4 | 20 |
| β-strand | 150-152 | 3 | 21 |
| β-strand | 155-157 | 3 | 19 |
| α-helix | 161-162 | 2 | |
| β-strand | 163-168 | 6 | 20 |
| β-strand | 171-172 | 2 | 20 |
| β-strand | 182-184 | 3 | 21 |
| β-strand | 199-201 | 3 | 21 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-217 | 8 | 20 |
| β-strand | 222-224 | 3 | 20 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-233 | 6 | 20 |
| α-helix | 234-235 | 2 | |
| β-strand | 241-247 | 7 | 22 |
| α-helix | 248-251 | 4 | |
| β-strand | 252-254 | 3 | 23 |
| β-strand | 259-269 | 11 | 22 |
| α-helix | 271-272 | 2 | |
| β-strand | 273-278 | 6 | 23 |
| β-strand | 281-282 | 2 | 23 |
| β-strand | 291 | 1 | 23 |
| β-strand | 293-299 | 7 | 22 |
| β-strand | 305-313 | 9 | 23 |
| β-strand | 316-326 | 11 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-35 | 2 | |
| β-strand | 39-41 | 3 | 24 |
| β-strand | 47-50 | 4 | 24 |
| α-helix | 59-60 | 2 | |
| β-strand | 67-71 | 5 | 24 |
| β-strand | 79-80 | 2 | 25 |
| β-strand | 93-95 | 3 | 24 |
| β-strand | 103-104 | 2 | 25 |
| β-strand | 117-119 | 3 | 24 |
| β-strand | 127-128 | 2 | 26 |
| β-strand | 141-143 | 3 | 24 |
| β-strand | 151-152 | 2 | 26 |
| α-helix | 153 | 1 | |
| α-helix | 158-160 | 3 | |
| β-strand | 166-168 | 3 | 24 |
| α-helix | 179-182 | 4 | |
| β-strand | 190-192 | 3 | 24 |
| β-strand | 214-216 | 3 | 24 |
| β-strand | 246-248 | 3 | 24 |
| β-strand | 254-255 | 2 | 27 |
| α-helix | 258-260 | 3 | |
| α-helix | 261-264 | 4 | |
| β-strand | 274 | 1 | 28 |
| β-strand | 275-277 | 3 | 27 |
| α-helix | 279-281 | 3 | |
| β-strand | 285 | 1 | 28 |
| α-helix | 286-288 | 3 | |
| α-helix | 291-293 | 3 | |
| β-strand | 297-303 | 7 | 29 |
| β-strand | 319 | 1 | 30 |
| β-strand | 322-326 | 5 | 29 |
| α-helix | 328-329 | 2 | |
| β-strand | 330-333 | 4 | 31 |
| β-strand | 349 | 1 | 30 |
| β-strand | 355 | 1 | 30 |
| β-strand | 367-374 | 8 | 31 |
| β-strand | 377-384 | 8 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor-type tyrosine-protein phosphatase delta | A, C | protein | 313 | Mus musculus | Q64487 (AlphaFold model) |
| Leucine-rich repeat and fibronectin type III domain-containing protein 1 | B, D | protein | 365 | Mus musculus | Q2WF71 (AlphaFold model) |
>5XWU_1 Receptor-type tyrosine-protein phosphatase delta (chains A, C) LMGCVAETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEF DDGSGSVLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQL KVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSESIGGTPIRGALQI EQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVN ITCVAVGSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAI AQITVKAHHHHHH
>5XWU_2 Leucine-rich repeat and fibronectin type III domain-containing protein 1 (chains B, D) QPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSL VHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRK VESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHK LVRLDMTSNRLHKLPPDGLFLRSQGGGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDD LETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVV HWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLH HHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Water and common crystallization additives (MES) are not listed.
Structural basis of trans-synaptic interactions between PTP delta and SALMs for inducing synapse formation. Goto-Ito, S., Yamagata, A., Sato, Y. et al. Nat Commun (2018) 9:269-269. DOI 10.1038/s41467-017-02417-z · PubMed
Other PDB entries of the same protein (UniProt Q64487 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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