6XVT: ENAH EVH1

ENAH EVH1 in complex with Ac-[2-Cl-F]-PPPPTEDDL-NH2. Determined by X-ray diffraction at 1.4 Å resolution. Released 18 Mar 2020.

Method: X-ray diffraction
Resolution: 1.4 Å
Organisms: Homo sapiens, synthetic construct
Chains: 4
Atoms: 2,100
Mol. weight: 26.92 kDa
Released: 18 Mar 2020

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

Secondary structure: helices and β-sheets

6XVT contains 5 α-helices and 16 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: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	3-17	15	1
β-strand	22-25	4	1
α-helix	26-28	3
β-strand	32-40	9	1
β-strand	45-52	8	1
β-strand	58-63	6	1
β-strand	71-72	2	1
β-strand	77-81	5	1
β-strand	86-91	6	1
α-helix	94-110	17

Chain B: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-17	14	2
β-strand	22-25	4	2
α-helix	26-28	3
β-strand	33-40	8	2
β-strand	45-52	8	2
β-strand	58-63	6	2
β-strand	71-72	2	2
β-strand	77-81	5	2
β-strand	86-91	6	2
α-helix	94-110	17

Chain H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein enabled homolog	A, B	protein	113	Homo sapiens	Q8N8S7 (AlphaFold model)
Acy-SC1-SC2-SC3-SC4-SC5-nme	G, H	protein	6	synthetic construct

Sequence of entity 1 (A, B), FASTA

>6XVT_1 Protein enabled homolog (chains A, B)
GSMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQV
VINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVL

Sequence of entity 2 (G, H), FASTA

>6XVT_2 ACY-SC1-SC2-SC3-SC4-SC5-NME (chains G, H)
XXPPPX

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
6RD2 1.0 Å, ENAH EVH1 in complex with Ac-[2-Cl-F]-[ProM-2]-[ProM-1]-TEDEL-NH2
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
9C66 1.4 Å, Structure of the Mena EVH1 domain bound to the polyproline segment of PTP1B

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