6RD2: ENAH EVH1

ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-1]-TEDEL-NH2. Determined by X-ray diffraction at 1.0 Å resolution. Released 13 May 2020.

Method: X-ray diffraction
Resolution: 1.0 Å
Organisms: Homo sapiens, synthetic construct
Chains: 4
Atoms: 2,313
Mol. weight: 28.72 kDa
Ligands: K1N
Released: 13 May 2020

Explore 6RD2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6RD2 contains 7 α-helices and 16 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: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-17	14	2
α-helix	18-20	3
β-strand	22-25	4	2
α-helix	26-28	3
β-strand	33-40	8	2
α-helix	41-43	3
β-strand	45-52	8	2
β-strand	58-63	6	2
β-strand	71	1	2
β-strand	77-81	5	2
β-strand	86-91	6	2
α-helix	94-110	17

Chain B: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-17	14	1
α-helix	18-20	3
β-strand	22-25	4	1
α-helix	26-28	3
β-strand	33-40	8	1
β-strand	45-52	8	1
β-strand	58-63	6	1
β-strand	71	1	1
β-strand	77-81	5	1
β-strand	86-91	6	1
α-helix	94-110	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein enabled homolog	A, B	protein	113	Homo sapiens	Q8N8S7 (AlphaFold model)
Thr-glu-asp-glu-nlw	C, D	protein	5	synthetic construct

Sequence of entity 1 (A, B), FASTA

>6RD2_1 Protein enabled homolog (chains A, B)
GSMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQV
VINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVL

Sequence of entity 2 (C, D), FASTA

>6RD2_2 THR-GLU-ASP-GLU-NLW (chains C, D)
TEDEL

Ligands and cofactors

ID	Name	Formula	Copies
K1N	(3~{S},7~{R},10~{R},13~{S})-4-[(3~{S},6~{R},8~{a}~{S})-1'-[(2~{S})-2-acetamido-…	C35 H40 Cl N5 O7	2

Water and common crystallization additives (NO3, GOL) are not listed.

Primary citation

Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells. Barone, M., Muller, M., Chiha, S. et al. Proc Natl Acad Sci U S A (2020) 117:29684-29690. DOI 10.1073/pnas.2007213117 · PubMed

Other PDB entries of the same protein (UniProt Q8N8S7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7A5M 0.78 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-17]-OMe
5NCG 1.02 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-9]-OH
6RCF 1.1 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-15]-OH
5NBF 1.15 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-3]-OH
5N9C 1.16 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-PP-[ProM-1]-OH
5NEG 1.29 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-13]-OEt
2HO2 1.33 Å, Structure of human FE65-WW domain in complex with hMena peptide.
6RCJ 1.35 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-15]-OMe
7AKI 1.36 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-1]-NH2
5NCF 1.4 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-4]-OH
6XVT 1.4 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-PPPPTEDDL-NH2
9C66 1.4 Å, Structure of the Mena EVH1 domain bound to the polyproline segment of PTP1B

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