4Y21: Munc13-1 MUN domain

Crystal Structure of Munc13-1 MUN domain. Determined by X-ray diffraction at 2.9 Å resolution. Released 10 Jun 2015.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 4,347
Mol. weight: 61.99 kDa
Released: 10 Jun 2015

Explore 4Y21 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Y21 contains 34 α-helices and 4 β-strands across 1 chain. 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: 34 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	11-29	19
α-helix	32-35	4
α-helix	41-63	23
α-helix	73-94	22
α-helix	96-103	8
α-helix	118	1
α-helix	122	1
α-helix	127-142	16
α-helix	143-147	5
α-helix	148-150	3
α-helix	160-186	27
α-helix	191-204	14
α-helix	205-209	5
α-helix	213-216	4
α-helix	222-245	24
α-helix	249-254	6
β-strand	259	1	1
β-strand	267	1	1
α-helix	268-286	19
α-helix	292-321	30
α-helix	322-324	3
α-helix	327-329	3
α-helix	331-353	23
α-helix	361-387	27
α-helix	390-405	16
α-helix	418-420	3
α-helix	421-443	23
α-helix	444-446	3
α-helix	449-470	22
α-helix	474-476	3
β-strand	477-480	4	2
β-strand	483-486	4	2
α-helix	487-489	3
α-helix	491-493	3
α-helix	494-512	19
α-helix	520-525	6
α-helix	527-539	13
α-helix	544-545	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein unc-13 homolog A	A	protein	539	Rattus norvegicus	Q62768 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4Y21_1 Protein unc-13 homolog A (chains A)
GKERFVKLLDQLHNSLRIDLSMYRNNFPASSPERLQDLKSTVDLLTSITFFRMKVQELQS
PPRASQVVKDCVKACLNSTYEYIFNNCHELYGREYQTDPAKKGEVPPEEQGPSIKNLDFW
SKLITLIVSIIEEDKNSYTPCLNQFPQELNVGKISAEVMWSLFAQDMKYAMEEHDKHRLC
KSADYMNLHFKVKWLYNEYVAELPTFKDRVPEYPAWFEPFVIQWLDENEEVSRDFLHGAL
ERDKKDGFQQTSEHALFSCSVVDVFSQLNQSFEIIKKLECPDPQIVGHYMRRFAKTISNV
LLQYADIVSKDFASYCSKEKEKVPCILMNNTQQLRVQLEKMFEAMGGKELDAEASGTLKE
LQVKLNNVLDELSHVFATSFQPHIEECVRQMGDILSQVKGTGNVPASACSSVAQDADNVL
QPIMDLLDSNLTLFAKICEKTVLKRVLKELWKLVMNTMERTIVLPPEFSKLKDHMVREEA
KSLTPKQCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSLYTQATDLLIK

Primary citation

Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming. Yang, X., Wang, S., Sheng, Y. et al. Nat Struct Mol Biol (2015) 22:547-554. DOI 10.1038/nsmb.3038 · PubMed

Other PDB entries of the same protein (UniProt Q62768 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6NYT 1.37 Å, Munc13-1 C2B-domain, calcium bound
2CJT 1.44 Å, Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch:…
2CJS 1.78 Å, Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch:…
6NYC 1.89 Å, Munc13-1 C2B-domain, calcium free
3SWH 2.65 Å, Munc13-1, MUN domain, C-terminal module
6A30 2.79 Å, Crystal Structure of Munc13-1 MUN Domain and Synaptobrevin-2 Juxtamembrane Linker Region
5UF7 2.9 Å, Crystal structure of MUNC13-1 mun domain
5UE8 3.35 Å, The crystal structure of Munc13-1 C1C2BMUN domain
7T7X 10.0 Å, Munc13-1 C1-C2B-MUN-C2C Upright conformation spanning two lipid bilayers
7T81 10.0 Å, Model of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers.
1Y8F Solution structure of the munc13-1 C1-domain
2KDU Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin…

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