Cryo-EM structure of full length Neuroligin-2 from Mouse. Determined by electron microscopy at 3.28 Å resolution. Released 14 May 2025.
Explore 8G7D in 3D Show helices and sheets RCSB PDB PDBe
8G7D contains 54 α-helices and 33 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 | 43-45 | 3 | 1 |
| β-strand | 50-52 | 3 | 1 |
| β-strand | 54 | 1 | 2 |
| α-helix | 56-58 | 3 | |
| β-strand | 66-73 | 8 | 2 |
| α-helix | 89-92 | 4 | |
| β-strand | 96-98 | 3 | 1 |
| α-helix | 102-107 | 6 | |
| α-helix | 121-125 | 5 | |
| α-helix | 127-130 | 4 | |
| β-strand | 143-149 | 7 | 2 |
| α-helix | 176 | 1 | |
| β-strand | 177-183 | 7 | 2 |
| α-helix | 199-205 | 7 | |
| β-strand | 208-212 | 5 | 2 |
| α-helix | 218-221 | 4 | |
| α-helix | 233-252 | 20 | |
| β-strand | 254-264 | 11 | 2 |
| α-helix | 266-275 | 10 | |
| β-strand | 288-290 | 3 | 2 |
| β-strand | 301 | 1 | 3 |
| α-helix | 304-315 | 12 | |
| α-helix | 322-331 | 10 | |
| α-helix | 334-338 | 5 | |
| β-strand | 354 | 1 | 3 |
| α-helix | 364-369 | 6 | |
| β-strand | 378-383 | 6 | 2 |
| α-helix | 387-389 | 3 | |
| α-helix | 406-415 | 10 | |
| α-helix | 425-434 | 10 | |
| α-helix | 438-440 | 3 | |
| α-helix | 447-456 | 10 | |
| α-helix | 457-461 | 5 | |
| α-helix | 462-473 | 12 | |
| β-strand | 478-483 | 6 | 2 |
| α-helix | 504-507 | 4 | |
| α-helix | 525-544 | 20 | |
| β-strand | 573 | 1 | 4 |
| β-strand | 578 | 1 | 4 |
| β-strand | 581-583 | 3 | 2 |
| α-helix | 595-599 | 5 | |
| α-helix | 600-604 | 5 | |
| α-helix | 605-607 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 43-45 | 3 | 5 |
| β-strand | 50-52 | 3 | 5 |
| β-strand | 54 | 1 | 6 |
| β-strand | 66-70 | 5 | 6 |
| α-helix | 89-92 | 4 | |
| β-strand | 96-98 | 3 | 5 |
| α-helix | 102-107 | 6 | |
| α-helix | 121-125 | 5 | |
| α-helix | 127-133 | 7 | |
| β-strand | 144-149 | 6 | 6 |
| α-helix | 176 | 1 | |
| β-strand | 177-183 | 7 | 6 |
| α-helix | 193-195 | 3 | |
| α-helix | 199-205 | 7 | |
| β-strand | 208-212 | 5 | 6 |
| α-helix | 218-221 | 4 | |
| α-helix | 233-252 | 20 | |
| β-strand | 254-264 | 11 | 6 |
| α-helix | 266-275 | 10 | |
| β-strand | 286-290 | 5 | 6 |
| β-strand | 301 | 1 | 7 |
| α-helix | 304-315 | 12 | |
| α-helix | 322-331 | 10 | |
| α-helix | 334-338 | 5 | |
| β-strand | 354 | 1 | 7 |
| α-helix | 364-369 | 6 | |
| β-strand | 378-383 | 6 | 6 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-395 | 3 | |
| α-helix | 403-415 | 13 | |
| α-helix | 425-434 | 10 | |
| α-helix | 438-440 | 3 | |
| α-helix | 447-456 | 10 | |
| α-helix | 457-461 | 5 | |
| α-helix | 462-473 | 12 | |
| β-strand | 478-483 | 6 | 6 |
| α-helix | 504-507 | 4 | |
| α-helix | 525-543 | 19 | |
| α-helix | 570-572 | 3 | |
| β-strand | 580-583 | 4 | 6 |
| β-strand | 589-590 | 2 | 6 |
| α-helix | 595-599 | 5 | |
| α-helix | 600-604 | 5 | |
| α-helix | 605-607 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuroligin-1,Neuroligin-2 | A, B | protein | 870 | Mus musculus | Q69ZK9 (AlphaFold model), Q99K10 (AlphaFold model) |
>8G7D_1 Neuroligin-1,Neuroligin-2 (chains A, B) MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKYPYDVPDYAQRGG GGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPP LGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQS EDCLYLNLYVPTEDDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVVTLNYR LGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLI LSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSR ELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSA ESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALF TDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGA TDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNS KEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPG PGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAF AALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVG ADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPP PPPTATSHNNTLPHPHSTTRVSNSLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Weaker neuroligin 2-neurexin beta 1 interaction tethers membranes and recruits gephyrin at membrane junctions through clustering. Boyd, R., Jaqaman, K., Wang, W. Sci Adv (2026) 12:eads9732-eads9732. DOI 10.1126/sciadv.ads9732 · PubMed
Other PDB entries of the same protein (UniProt Q69ZK9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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