4MT6: Closed inactive collybistin

Crystal structure of closed inactive collybistin. Determined by X-ray diffraction at 5.5 Å resolution. Released 13 Aug 2014.

Method: X-ray diffraction
Resolution: 5.5 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 3,298
Mol. weight: 54.08 kDa
Released: 13 Aug 2014

Explore 4MT6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MT6 contains 19 α-helices and 15 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: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	19-22	4	1
β-strand	41-44	4	1
β-strand	53-56	4	1
β-strand	61-64	4	1
α-helix	66-68	3
β-strand	69-71	3	1
α-helix	108-131	24
α-helix	132-137	6
α-helix	138-142	5
α-helix	149-155	7
α-helix	159-176	18
α-helix	182-184	3
α-helix	188-193	6
α-helix	200-206	7
α-helix	208-219	12
α-helix	222-234	13
α-helix	242-245	4
α-helix	249-265	17
α-helix	274-299	26
α-helix	302-308	7
β-strand	312	1	2
α-helix	319-321	3
β-strand	326-335	10	2
α-helix	340-342	3
β-strand	343-350	8	2
β-strand	353-359	7	2
β-strand	367-374	8	2
β-strand	378-381	4	2
α-helix	383-384	2
β-strand	386-387	2	3
β-strand	394-395	2	3
β-strand	398-403	6	2
β-strand	409-413	5	2
α-helix	417-438	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho guanine nucleotide exchange factor 9	A	protein	456	Rattus norvegicus	Q9QX73 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4MT6_1 Rho guanine nucleotide exchange factor 9 (chains A)
MQWIRGGSGMLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDE
EGWFPASFVRLWVNQEDGVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMS
TERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNND
DPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDI
AIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLEN
IDKIAQWQASVLDWEGDDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKD
LIRRDILYYKGRIDMDKYEVIDIEDGRDDDFNVSMKNAFKLHNKETEEVHLFFAKKLEEK
IRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTV

Primary citation

A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. Soykan, T., Schneeberger, D., Tria, G. et al. EMBO J (2014) 33:2113-2133. DOI 10.15252/embj.201488143 · PubMed

Other PDB entries of the same protein (UniProt Q9QX73 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2DFK 2.15 Å, Crystal structure of the CDC42-Collybistin II complex
4MT7 3.5 Å, Crystal structure of collybistin I

Browse structure collections

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