7CSO: Ephexin4 DH-PH-SH3

Structure of Ephexin4 DH-PH-SH3. Determined by X-ray diffraction at 2.39 Å resolution. Released 24 Feb 2021.

Method: X-ray diffraction
Resolution: 2.39 Å
Organism: Mus musculus
Chains: 4
Atoms: 14,658
Mol. weight: 211.51 kDa
Released: 24 Feb 2021

Explore 7CSO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CSO contains 94 α-helices and 66 β-strands across 4 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: 23 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	278-280	3
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-322	5
α-helix	326-333	8
α-helix	336-356	21
α-helix	364-373	10
α-helix	376-383	8
α-helix	385-398	14
α-helix	400-411	12
α-helix	413-415	3
α-helix	420-424	5
α-helix	426-443	18
α-helix	449-488	40
β-strand	489-490	2	1
β-strand	506-514	9	1
α-helix	515	1
β-strand	529-535	7	1
β-strand	538-546	9	1
β-strand	549-557	9	1
α-helix	558-560	3
β-strand	561-565	5	1
α-helix	567-570	4
β-strand	585-591	7	1
β-strand	594	1	1
β-strand	600-606	7	1
α-helix	609-619	11
α-helix	632-634	3
β-strand	637-640	4	2
β-strand	644	1	3
β-strand	651	1	2
β-strand	654	1	3
β-strand	659-666	8	2
β-strand	669-674	6	2
β-strand	680-684	5	2
α-helix	685-687	3
β-strand	688-691	4	2
α-helix	694-707	14

Chain B: 24 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	278-280	3
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-321	4
α-helix	326-333	8
α-helix	336-356	21
α-helix	364-373	10
α-helix	376-383	8
α-helix	385-398	14
α-helix	400-410	11
α-helix	413-415	3
α-helix	420-424	5
α-helix	426-443	18
α-helix	449-488	40
β-strand	489-490	2	4
β-strand	506-514	9	4
α-helix	515	1
β-strand	529-535	7	4
β-strand	538-546	9	4
β-strand	549-557	9	4
α-helix	558-560	3
β-strand	561-565	5	4
α-helix	567-570	4
β-strand	585-591	7	4
β-strand	600-606	7	4
α-helix	609-619	11
α-helix	621-623	3
α-helix	632-634	3
β-strand	637-640	4	5
β-strand	644	1	6
β-strand	651	1	5
β-strand	654	1	6
β-strand	659-666	8	5
β-strand	669-674	6	5
β-strand	680-684	5	5
α-helix	685-687	3
β-strand	688-690	3	5
α-helix	694-707	14

Chain C: 23 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	278-280	3
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-321	4
α-helix	326-333	8
α-helix	336-356	21
α-helix	364-373	10
α-helix	376-383	8
α-helix	385-398	14
α-helix	400-410	11
α-helix	413-415	3
α-helix	420-424	5
α-helix	426-443	18
α-helix	449-488	40
β-strand	489-490	2	7
β-strand	506-514	9	7
α-helix	515	1
β-strand	529-535	7	7
β-strand	538-546	9	7
β-strand	549-557	9	7
α-helix	558-560	3
β-strand	561-565	5	7
β-strand	585-591	7	7
β-strand	594	1	7
β-strand	600-606	7	7
α-helix	609-619	11
α-helix	632-634	3
β-strand	637-640	4	8
β-strand	644	1	9
β-strand	651	1	8
β-strand	654	1	9
β-strand	659-666	8	8
β-strand	669-674	6	8
β-strand	680-684	5	8
α-helix	685-687	3
β-strand	688-690	3	8
α-helix	694-707	14
α-helix	709-710	2

Chain D: 24 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	278-280	3
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-322	5
α-helix	326-333	8
α-helix	336-356	21
α-helix	364-373	10
α-helix	376-383	8
α-helix	385-398	14
α-helix	400-411	12
α-helix	413-415	3
α-helix	420-424	5
α-helix	426-443	18
α-helix	449-488	40
β-strand	489-490	2	10
β-strand	506-514	9	10
α-helix	515	1
β-strand	529-535	7	10
β-strand	538-546	9	10
β-strand	549-557	9	10
α-helix	558-560	3
β-strand	561-565	5	10
α-helix	567-571	5
β-strand	585-591	7	10
β-strand	600-606	7	10
α-helix	609-619	11
α-helix	622-624	3
α-helix	632-634	3
β-strand	637-640	4	11
β-strand	644	1	12
β-strand	651	1	11
β-strand	654	1	12
β-strand	659-666	8	11
β-strand	669-674	6	11
β-strand	680-684	5	11
α-helix	685-687	3
β-strand	688-690	3	11
α-helix	694-707	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho guanine nucleotide exchange factor 16	A, B, C, D	protein	459	Mus musculus	Q3U5C8 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7CSO_1 Rho guanine nucleotide exchange factor 16 (chains A, B, C, D)
GPGSGPRPAQLTWSQLPEVLESGVLDTLSTEERKRQEAIFEILTSEFSYLHSLSILVTEF
LQSRELRATMTQTEHHHLFSNILDVMSASQKFFEALEQRHKAQVCVEDISDILEDHAQHH
FHPYIAYCSNEVYQQRTLQKLSNSNAAFRDVLKEIEKRPACGGLPMISFLILPMQRVTRL
PLLTDTLCLKTQGHPERYKAASQALKAISKLVKQCNEGAHKMERTEQIYTLNMQLDFGKV
KSLPLISASRWLLKRGELFLLEESSIFRKIASRPTCYLFLFNDVLVVTKKKSEESYLVQD
YAQLDHVQVRKLEPSEPLLPGGSSRSSSVPYPFQVNLLHNSEGRQEQILLSSDSASDRAR
WITALTYKERQWQGITNKGELPQVEVTKAYFAKQADEITLQQADIVLVLQEEDGWLHGER
LRDGETGWFPESFAHSITSRVAVEGNVRRMERLRVETDV

Primary citation

Double inhibition and activation mechanisms of Ephexin family RhoGEFs. Zhang, M., Lin, L., Wang, C. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2024465118 · PubMed

Other PDB entries of the same protein (UniProt Q3U5C8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7YKF 2.28 Å, Crystal structure of MAGI2 PDZ0-GK/pEphexin4 complex
7CSP 3.0 Å, Structure of Ephexin4 IDPSH
7CSR 3.0 Å, Structure of Ephexin4 R676L

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