2CJS: Unc-13 homolog a

Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch: C2-domains as Versatile Protein-Protein Interaction Modules. Determined by X-ray diffraction at 1.78 Å resolution. Released 7 Jun 2006.

Method: X-ray diffraction
Resolution: 1.78 Å
Organism: RATTUS NORVEGICUS
Chains: 3
Atoms: 3,542
Mol. weight: 45 kDa
Ligands: ZN
Released: 7 Jun 2006

Explore 2CJS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CJS contains 13 α-helices and 27 β-strands across 3 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: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	-7--6	2	1
β-strand	3-12	10	2
α-helix	17-19	3
β-strand	21-28	8	2
β-strand	31-34	4	2
α-helix	35-37	3
β-strand	38-39	2	2
β-strand	44-52	9	2
β-strand	59-66	8	2
β-strand	73-81	9	2
α-helix	82-84	3
α-helix	86	1
β-strand	87	1	2
β-strand	95-106	12	2
β-strand	109-128	20	2
α-helix	129-134	6
α-helix	135-153	19

Chain B: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	2-12	11	1
α-helix	17-19	3
β-strand	21-28	8	1
β-strand	31-34	4	1
β-strand	38-39	2	1
β-strand	44-53	10	1
β-strand	59-66	8	1
β-strand	72-81	10	1
α-helix	82-84	3
β-strand	86-87	2	1
β-strand	95-105	11	1
β-strand	110-128	19	1
α-helix	129-130	2
α-helix	135-145	11

Chain C: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	91	1	2
α-helix	98	1
β-strand	99-100	2	2
α-helix	101	1
β-strand	106-107	2	3
β-strand	114-115	2	3
β-strand	120-125	6	1
β-strand	129-134	6	1
α-helix	135-141	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Unc-13 homolog a	A, B	protein	167	RATTUS NORVEGICUS	Q62768 (AlphaFold model)
Regulating synaptic membrane exocytosis protein 2	C	protein	62	RATTUS NORVEGICUS	Q9JIS1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2CJS_1 UNC-13 HOMOLOG A (chains A, B)
GSPGISGGGGGILSLLCVGVKKAKFDGAQEKFNTYVTLKVQNVESTTIAVRGSQPSWEQD
FMFEINRLDLGLTVEVWNKGLIWDTMVGTVWIPLRTIRQSNEEGPGEWLTLDSQAIMADS
EICGTKDPTFHRILLDAHFELPLDIPEEEARYWAKKLEQLNAKLNSS

Sequence of entity 2 (C), FASTA

>2CJS_2 REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2 (chains C)
GSQEQKGDAPTCGICHKTKFADGCGHNCSYCQTKFCARCGGRVSLRSNKVMWVCNLCRKQ
QE

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Water and common crystallization additives (EDO, GOL) are not listed.

Primary citation

Structural Basis for a Munc13-1 Homodimer to Munc13-1/Rim Heterodimer Switch. Lu, J., Machius, M., Dulubova, I. et al. PLoS Biol (2006) 4:E192. DOI 10.1371/JOURNAL.PBIO.0040192 · 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:…
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
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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