Research workbench

Structure of EPHEXIN4 dh-pH-SH3

Analyse Structure of EPHEXIN4 dh-pH-SH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CSO
Type: protein
Length: 1,736 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q3U5C8
Ligands: SO4

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	432	—	Q3U5C8
B	—	protein	433	—	Q3U5C8
C	—	protein	437	—	Q3U5C8
D	—	protein	434	—	Q3U5C8

Ligands and binding sites

SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D

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

Compared structures

7CSO · Structure of Ephexin4 DH-PH-SH3 · the same entry in another collection · chain D against D, TM-score 1.00
Q3U5C8 · AlphaFold monomer V2.0 prediction for rho guanine nucleotide exchange factor 16 (Q3U5C8) · a predicted model of the same protein · chain C against A, TM-score 0.68

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 Q3U5C8
Elsewhere: RCSB PDB 7CSO · PDBe 7CSO · UniProt Q3U5C8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.