5UE8: Munc13-1 C1C2BMUN domain

The crystal structure of Munc13-1 C1C2BMUN domain. Determined by X-ray diffraction at 3.35 Å resolution. Released 15 Feb 2017.

Method: X-ray diffraction
Resolution: 3.35 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 13,603
Mol. weight: 219.74 kDa
Ligands: ZN
Released: 15 Feb 2017

Explore 5UE8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UE8 contains 88 α-helices and 28 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.

Chain A: 43 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	544-558	15
α-helix	565-567	3
β-strand	569-572	4	1
β-strand	578-579	2	2
β-strand	586-587	2	2
α-helix	590-592	3
β-strand	594-597	4	1
β-strand	603-604	2	1
α-helix	609-611	3
α-helix	616-627	12
α-helix	630-650	21
α-helix	653-661	9
α-helix	666-680	15
β-strand	690-699	10	3
β-strand	712-718	7	4
β-strand	721-724	4	4
α-helix	725-728	4
β-strand	735-743	9	3
β-strand	751-757	7	4
α-helix	775	1
β-strand	776-783	8	4
β-strand	791-797	7	3
α-helix	798	1
β-strand	799	1	4
β-strand	810-818	9	3
α-helix	828-841	14
α-helix	842-847	6
α-helix	872-880	9
α-helix	886-897	12
α-helix	898-900	3
α-helix	906-920	15
α-helix	932-936	5
α-helix	943-961	19
α-helix	964-967	4
α-helix	973-992	20
α-helix	993-997	5
α-helix	1005-1026	22
α-helix	1028-1035	8
α-helix	1059-1074	16
α-helix	1075-1079	5
α-helix	1080-1082	3
α-helix	1092-1118	27
α-helix	1123-1136	14
α-helix	1137-1141	5
α-helix	1145-1148	4
α-helix	1155-1187	33
α-helix	1201-1218	18
α-helix	1224-1251	28
α-helix	1264-1285	22
α-helix	1288-1290	3
α-helix	1293-1319	27
α-helix	1322-1336	15
α-helix	1354-1375	22
α-helix	1381-1398	18
α-helix	1471-1487	17
α-helix	1495-1499	5
α-helix	1502-1511	10

Chain B: 45 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	544-558	15
α-helix	565-567	3
β-strand	569-572	4	5
β-strand	578-579	2	6
β-strand	586-587	2	6
α-helix	590-592	3
β-strand	594-597	4	5
β-strand	603-604	2	5
α-helix	609-611	3
α-helix	616-624	9
α-helix	632-650	19
α-helix	653-661	9
α-helix	666-680	15
β-strand	690-699	10	7
β-strand	712-718	7	8
β-strand	721-724	4	8
α-helix	725-728	4
β-strand	735-741	7	7
β-strand	750-757	8	8
β-strand	776-784	9	8
α-helix	785-787	3
β-strand	791-797	7	7
α-helix	798	1
β-strand	799	1	8
β-strand	810-818	9	7
α-helix	828-842	15
α-helix	843-847	5
α-helix	872-882	11
α-helix	886-897	12
α-helix	898-900	3
α-helix	906-918	13
α-helix	933-937	5
α-helix	943-961	19
α-helix	964-967	4
α-helix	973-992	20
α-helix	993-997	5
α-helix	1005-1025	21
α-helix	1028-1035	8
α-helix	1059-1074	16
α-helix	1075-1079	5
α-helix	1080-1082	3
α-helix	1092-1118	27
α-helix	1123-1136	14
α-helix	1137-1141	5
α-helix	1154-1187	34
α-helix	1201-1217	17
α-helix	1224-1251	28
α-helix	1254-1256	3
α-helix	1264-1285	22
α-helix	1288-1290	3
α-helix	1293-1319	27
α-helix	1322-1336	15
α-helix	1355-1365	11
α-helix	1366-1371	6
α-helix	1372-1378	7
α-helix	1381-1402	22
α-helix	1469-1487	19
α-helix	1495-1499	5
α-helix	1502-1514	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein unc-13 homolog A	A, B	protein	961	Rattus norvegicus	Q62768 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5UE8_1 Protein unc-13 homolog A (chains A, B)
AGITSALASSTLNNEELKNHVYKKTLQALIYPISCTTPHNFEVWTATTPTYCYECEGLLW
GIARQGMRCTECGVKCHEKCQDLLNADCLQRAAEKSSKHGAEDRTQNIIMVLKDRMKIRE
RNKPEIFELIQEVFAVTKSAHTQQMKAVKQSVLDGTSKWSAKISITVVCAQGLQAKDKTG
SSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVWDEDDDIKSRVKQ
RFKRESDDFLGQTIIEVRTLSGEMDVWYNLDKRTDKSAVSGAIRLHISVEIKGEEKVAPY
HVQYTCLHENLFHFVTDVQNNGVVKIPDAKGDDAWKVYYDETAQEIVDEFAMRYGVESIY
QAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVK
LLDQLHNSLRIDLSMYRNNFPASSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQV
VKDCVKACLNSTYEYIFNNCHELYGREYQTDPAKKGEVPPEEQGPSIKNLDFWSKLITLI
VSIIEEDKNSYTPCLNQFPQELNVGKISAEVMWSLFAQDMKYAMEEHDKHRLCKSADYMN
LHFKVKWLYNEYVAELPTFKDRVPEYPAWFEPFVIQWLDENEEVSRDFLHGALERDKKDG
FQQTSEHALFSCSVVDVFSQLNQSFEIIKKLECPDPQIVGHYMRRFAKTISNVLLQYADI
VSKDFASYCSKEKEKVPCILMNNTQQLRVQLEKMFEAMGGKELDAEASGTLKELQVKLNN
VLDELSHVFATSFQPHIEECVRQMGDILSQVKGTGNVPASACSSVAQDADNVLQPIMDLL
DSNLTLFAKICEKTVLKRVLKELWKLVMNTMERTIVLPPEFLSKLKDHMVREEAKSLTPK
QCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSLYTQATDLLIKTFVQTQS
A

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Water and common crystallization additives (CL) are not listed.

Primary citation

Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN. Xu, J., Camacho, M., Xu, Y. et al. Elife (2017) 6. DOI 10.7554/eLife.22567 · 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
4Y21 2.9 Å, Crystal Structure of Munc13-1 MUN 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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