Research workbench

The crystal structure of the second PDZ domain of human nherf-2 (SLC9A3R2) interacting with a mode 1 PDZ binding motif

Analyse The crystal structure of the second PDZ domain of human nherf-2 (SLC9A3R2)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HE4
Type: protein
Length: 90 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NA(+)/H(+) exchange regulatory cofactor nhe-RF2
UniProt: Q15599
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NA(+)/H(+) exchange regulatory cofactor nhe-RF2	protein	90	14% helix, 37% strand	Q15599

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.29	0.75	12	empty

Compared structures

2HE4 · The crystal structure of the second PDZ domain of human NHERF-2 (SLC9A3R2) interacting… · the same entry in another collection · chain A against A, TM-score 1.00
Q15599 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF2… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q15599
Elsewhere: RCSB PDB 2HE4 · PDBe 2HE4 · UniProt Q15599

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