7CSR: Ephexin4 R676L

Structure of Ephexin4 R676L. Determined by X-ray diffraction at 3.0 Å resolution. Released 24 Feb 2021.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Mus musculus
Chains: 3
Atoms: 10,175
Mol. weight: 157.56 kDa
Released: 24 Feb 2021

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

Secondary structure: helices and β-sheets

7CSR contains 58 α-helices and 48 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: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-323	6
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	426-444	19
α-helix	449-488	40
β-strand	489-490	2	1
β-strand	506-514	9	1
β-strand	529-535	7	1
β-strand	538-544	7	1
β-strand	550-557	8	1
α-helix	558-560	3
β-strand	561-565	5	1
α-helix	566-567	2
β-strand	586-591	6	1
β-strand	600-605	6	1
α-helix	609-619	11
β-strand	637-640	4	2
β-strand	644	1	3
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: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	271-276	6
α-helix	284-310	27
α-helix	311-315	5
α-helix	318-323	6
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	4
β-strand	506-514	9	4
β-strand	529-535	7	4
β-strand	538-544	7	4
β-strand	550-557	8	4
α-helix	558-560	3
β-strand	561-565	5	4
β-strand	586-591	6	4
β-strand	600-605	6	4
α-helix	609-619	11
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	696-700	5

Chain C: 20 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	267-269	3
α-helix	271-276	6
α-helix	284-309	26
α-helix	310-315	6
α-helix	318-323	6
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	400-409	10
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
β-strand	529-535	7	7
β-strand	538-544	7	7
β-strand	550-557	8	7
α-helix	558-560	3
β-strand	561-565	5	7
α-helix	567-571	5
β-strand	586-591	6	7
β-strand	594	1	7
β-strand	600-605	6	7
α-helix	609-619	11
β-strand	637-639	3	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	689-690	2	8
α-helix	694-707	14

Molecules and chains

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

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

>7CSR_1 Rho guanine nucleotide exchange factor 16 (chains A, B, C)
GPGSGPRPAQLTWSQLPEVLESGVLDTLSTEERKRQEAIFEILTSEFSYLHSLSILVTEF
LQSRELRATMTQTEHHHLFSNILDVMSASQKFFEALEQRHKAQVCVEDISDILEDHAQHH
FHPYIAYCSNEVYQQRTLQKLSNSNAAFRDVLKEIEKRPACGGLPMISFLILPMQRVTRL
PLLTDTLCLKTQGHPERYKAASQALKAISKLVKQCNEGAHKMERTEQIYTLNMQLDFGKV
KSLPLISASRWLLKRGELFLLEESSIFRKIASRPTCYLFLFNDVLVVTKKKSEESYLVQD
YAQLDHVQVRKLEPSEPLLPGGSSRSSSVPYPFQVNLLHNSEGRQEQILLSSDSASDRAR
WITALTYKERQWQGITNKGELPQVEVTKAYFAKQADEITLQQADIVLVLQEEDGWLHGER
LLDGETGWFPESFAHSITSRVAVEGNVRRMERLRVETDV

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
7CSO 2.39 Å, Structure of Ephexin4 DH-PH-SH3
7CSP 3.0 Å, Structure of Ephexin4 IDPSH

Browse structure collections

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