Crystal structure of the complex between Slitrk2 LRR1 and PTP delta Ig1-Fn1. Determined by X-ray diffraction at 3.36 Å resolution. Released 3 Jun 2015.
Explore 4Y61 in 3D Show helices and sheets RCSB PDB PDBe
4Y61 contains 21 α-helices and 53 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.
| 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 | 2 |
| β-strand | 69-70 | 2 | 2 |
| β-strand | 76-80 | 5 | 1 |
| β-strand | 86-91 | 6 | 1 |
| β-strand | 101-109 | 9 | 2 |
| β-strand | 112-123 | 12 | 2 |
| α-helix | 125-127 | 3 | |
| α-helix | 128-129 | 2 | |
| β-strand | 134-137 | 4 | 3 |
| β-strand | 142-145 | 4 | 4 |
| β-strand | 150-157 | 8 | 3 |
| α-helix | 161-162 | 2 | |
| β-strand | 163-168 | 6 | 4 |
| β-strand | 171-172 | 2 | 4 |
| α-helix | 173-174 | 2 | |
| β-strand | 182-185 | 4 | 3 |
| α-helix | 194 | 1 | |
| β-strand | 195-201 | 7 | 3 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-218 | 9 | 4 |
| β-strand | 221-224 | 4 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-233 | 6 | 4 |
| α-helix | 234-237 | 4 | |
| β-strand | 241-247 | 7 | 5 |
| β-strand | 252-254 | 3 | 6 |
| β-strand | 260-269 | 10 | 5 |
| α-helix | 271-272 | 2 | |
| β-strand | 273-278 | 6 | 6 |
| β-strand | 281-282 | 2 | 6 |
| β-strand | 291 | 1 | 6 |
| β-strand | 293-298 | 6 | 5 |
| β-strand | 305-313 | 9 | 6 |
| β-strand | 316-326 | 11 | 6 |
| α-helix | 331-333 | 3 | |
| β-strand | 334-342 | 9 | 7 |
| β-strand | 345-351 | 7 | 7 |
| α-helix | 357-358 | 2 | |
| β-strand | 360-366 | 7 | 8 |
| α-helix | 373-374 | 2 | |
| β-strand | 375-380 | 6 | 8 |
| β-strand | 384-388 | 5 | 7 |
| α-helix | 390-391 | 2 | |
| β-strand | 396-403 | 8 | 8 |
| β-strand | 408 | 1 | 8 |
| β-strand | 415-417 | 3 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-37 | 4 | 9 |
| β-strand | 42-45 | 4 | 9 |
| β-strand | 65-68 | 4 | 9 |
| β-strand | 76-77 | 2 | 10 |
| β-strand | 88-92 | 5 | 9 |
| β-strand | 100-101 | 2 | 10 |
| β-strand | 114-116 | 3 | 9 |
| β-strand | 124-125 | 2 | 11 |
| β-strand | 138-140 | 3 | 9 |
| β-strand | 148-149 | 2 | 11 |
| α-helix | 151-154 | 4 | |
| β-strand | 162-164 | 3 | 9 |
| β-strand | 185-187 | 3 | 9 |
| α-helix | 198-202 | 5 | |
| α-helix | 203-204 | 2 | |
| β-strand | 210-212 | 3 | 9 |
| β-strand | 218-219 | 2 | 12 |
| α-helix | 222-224 | 3 | |
| α-helix | 225-233 | 9 | |
| β-strand | 242 | 1 | 13 |
| β-strand | 243-245 | 3 | 12 |
| α-helix | 247-249 | 3 | |
| β-strand | 253 | 1 | 13 |
| α-helix | 259-262 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor-type tyrosine-protein phosphatase delta | A | protein | 398 | Mus musculus | Q64487 (AlphaFold model) |
| SLIT and NTRK-like protein 2 | B | protein | 272 | Mus musculus | Q810C0 (AlphaFold model) |
>4Y61_1 Receptor-type tyrosine-protein phosphatase delta (chains A) ETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGS VLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERT RTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSESIGGTPIRGALQIEQSEES DQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAV GSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVK ALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSV AGLSPYSDYEFRVVAVNNIGRGPASEPVLTQKHHHHHH
>4Y61_2 SLIT and NTRK-like protein 2 (chains B) MLSGVWFLSVLTVAGILQTESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPP QYRIYQLFLNGNLLTRLYPNEFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNN KLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKLKVLILNDNLLLSLPSNVFRF VLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGE IVCETPFRLHGKDVTQLTRQDLCPRKHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Structure of Slitrk2-PTP delta complex reveals mechanisms for splicing-dependent trans-synaptic adhesion. Yamagata, A., Sato, Y., Goto-Ito, S. et al. Sci Rep (2015) 5:9686-9686. DOI 10.1038/srep09686 · 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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