Research workbench

Falafel EVH1 domain bound to cenp-C fim

Analyse Falafel EVH1 domain bound to cenp-C fim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WSF
Type: protein
Length: 122 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein phosphatase 4 regulatory subunit 3; Cenp-C
UniProt: Q9VFS5, Q9VHP9
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein phosphatase 4 regulatory subunit 3	protein	111	16% helix, 48% strand	Q9VFS5
B	Cenp-C	protein	11	0% helix, 0% strand	Q9VHP9

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 732 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4WSF · Falafel EVH1 domain bound to CENP-C FIM · the same entry in another collection · chain A against A, TM-score 1.00
Q9VFS5 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 4 regulatory… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9VFS5
Every structure of UniProt Q9VHP9
Elsewhere: RCSB PDB 4WSF · PDBe 4WSF · UniProt Q9VFS5 · UniProt Q9VHP9

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