Research workbench

Active structure of EHD4 complexed with ADP

Analyse Active structure of EHD4 complexed with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MVF
Type: protein
Length: 375 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eh domain-containing protein 4
UniProt: Q9EQP2
Ligands: ADP, MG
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eh domain-containing protein 4	protein	375	56% helix, 11% strand	Q9EQP2

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.60	0.81	31	empty
2	304	0.57	0.77	34	empty
3	159	0.52	0.79	28	ADP, MG

Compared structures

5MVF · Active structure of EHD4 complexed with ADP · the same entry in another collection · chain A against A, TM-score 1.00
Q9EQP2 · AlphaFold monomer V2.0 prediction for eh domain-containing protein 4 (Q9EQP2) · a predicted model of the same protein · chain A against A, TM-score 0.67

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 Q9EQP2
Elsewhere: RCSB PDB 5MVF · PDBe 5MVF · UniProt Q9EQP2

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