Crystal Structure of rat Munc18-1 with K332E/K333E mutation. Determined by X-ray diffraction at 3.4 Å resolution. Released 15 Jul 2020.
Explore 6LPC in 3D Show helices and sheets RCSB PDB PDBe
6LPC contains 53 α-helices and 48 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 |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 15-19 | 5 | |
| α-helix | 20-22 | 3 | |
| β-strand | 29-32 | 4 | 1 |
| α-helix | 35-44 | 10 | |
| α-helix | 47-49 | 3 | |
| β-strand | 55-59 | 5 | 1 |
| β-strand | 73-75 | 3 | 1 |
| β-strand | 76 | 1 | 2 |
| α-helix | 81-90 | 10 | |
| β-strand | 102-104 | 3 | 3 |
| β-strand | 105 | 1 | 2 |
| α-helix | 112-119 | 8 | |
| α-helix | 122-125 | 4 | |
| β-strand | 127-130 | 4 | 3 |
| β-strand | 138-141 | 4 | 4 |
| β-strand | 144-146 | 3 | 4 |
| α-helix | 151-157 | 7 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-182 | 18 | |
| β-strand | 188-191 | 4 | 4 |
| α-helix | 196-213 | 18 | |
| α-helix | 224-226 | 3 | |
| β-strand | 229-234 | 6 | 4 |
| α-helix | 235-237 | 3 | |
| β-strand | 248 | 1 | 5 |
| α-helix | 249-256 | 8 | |
| β-strand | 260 | 1 | 6 |
| β-strand | 263-265 | 3 | 6 |
| β-strand | 278-280 | 3 | 6 |
| α-helix | 286-291 | 6 | |
| β-strand | 295 | 1 | 5 |
| α-helix | 299-310 | 12 | |
| α-helix | 328-358 | 31 | |
| α-helix | 362-373 | 12 | |
| β-strand | 376 | 1 | 7 |
| β-strand | 382 | 1 | 7 |
| α-helix | 383 | 1 | |
| α-helix | 387-395 | 9 | |
| α-helix | 401-415 | 15 | |
| β-strand | 418 | 1 | 8 |
| α-helix | 421-428 | 8 | |
| α-helix | 434-437 | 4 | |
| α-helix | 441-446 | 6 | |
| β-strand | 451 | 1 | 8 |
| β-strand | 473 | 1 | 9 |
| β-strand | 476 | 1 | 9 |
| α-helix | 481-487 | 7 | |
| β-strand | 501 | 1 | 4 |
| β-strand | 536-542 | 7 | 4 |
| β-strand | 545-546 | 2 | 10 |
| α-helix | 547-560 | 14 | |
| β-strand | 564-565 | 2 | 4 |
| β-strand | 567-569 | 3 | 4 |
| β-strand | 572-573 | 2 | 10 |
| α-helix | 575-582 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 15-19 | 5 | |
| α-helix | 20-22 | 3 | |
| β-strand | 29-32 | 4 | 11 |
| α-helix | 35-44 | 10 | |
| α-helix | 47-50 | 4 | |
| β-strand | 55-59 | 5 | 11 |
| β-strand | 75 | 1 | 12 |
| β-strand | 104 | 1 | 12 |
| β-strand | 138-141 | 4 | 13 |
| β-strand | 144-146 | 3 | 13 |
| α-helix | 153-157 | 5 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-182 | 18 | |
| β-strand | 188-191 | 4 | 14 |
| α-helix | 196-213 | 18 | |
| α-helix | 224-227 | 4 | |
| β-strand | 229-234 | 6 | 14 |
| α-helix | 235-237 | 3 | |
| β-strand | 248 | 1 | 15 |
| α-helix | 249-256 | 8 | |
| β-strand | 260 | 1 | 16 |
| β-strand | 263-266 | 4 | 16 |
| β-strand | 277-280 | 4 | 16 |
| α-helix | 286-291 | 6 | |
| β-strand | 295 | 1 | 15 |
| α-helix | 299-310 | 12 | |
| α-helix | 329-358 | 30 | |
| α-helix | 362-373 | 12 | |
| α-helix | 378-380 | 3 | |
| α-helix | 387-395 | 9 | |
| α-helix | 401-415 | 15 | |
| α-helix | 420-428 | 9 | |
| α-helix | 434-441 | 8 | |
| α-helix | 444-446 | 3 | |
| β-strand | 473 | 1 | 17 |
| β-strand | 476 | 1 | 17 |
| α-helix | 481-487 | 7 | |
| β-strand | 536-542 | 7 | 14 |
| β-strand | 545-546 | 2 | 18 |
| α-helix | 547-560 | 14 | |
| β-strand | 564-565 | 2 | 14 |
| β-strand | 567-569 | 3 | 13 |
| β-strand | 572-573 | 2 | 18 |
| α-helix | 575-582 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Syntaxin-binding protein 1 | A, B | protein | 594 | Rattus norvegicus | P61765 (AlphaFold model) |
>6LPC_1 Syntaxin-binding protein 1 (chains A, B) MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVED INKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVK SRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLC ATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPS SPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVS QEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLEEMPQYQKELSKYSTHLHLAEDCMKHYQG TVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITE ENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTP IIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIF ILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
Munc13 activates the Munc18-1/syntaxin-1 complex and enables Munc18-1 to prime SNARE assembly. Wang, X., Gong, J., Zhu, L. et al. EMBO J (2020) 39:e103631-e103631. DOI 10.15252/embj.2019103631 · PubMed
Other PDB entries of the same protein (UniProt P61765 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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