Research workbench

Human CASK/LIN-2 PDZ domain

Analyse Human CASK/LIN-2 PDZ domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KWA
Type: protein
Length: 174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HCASK/LIN-2 protein
UniProt: O14936
Ligands: SO4
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HCASK/LIN-2 protein	protein	88	24% helix, 36% strand	O14936
B	HCASK/LIN-2 protein	protein	86	17% helix, 40% strand	O14936

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

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	74	0.37	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 606 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1KWA · Human CASK/LIN-2 PDZ domain · the same entry in another collection · chain A against A, TM-score 1.00
O14936 · AlphaFold monomer V2.0 prediction for peripheral plasma membrane protein cask (O14936) · a predicted model of the same protein · chain B against A, TM-score 0.87

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 O14936
Elsewhere: RCSB PDB 1KWA · PDBe 1KWA · UniProt O14936

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