Research workbench

Crystal Structure of the third PDZ domain of PSD-95 protein in the space group P21 at pH 4.0

Analyse Crystal Structure of the third PDZ domain of PSD-95 protein in the space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8AH6
Type: protein
Length: 203 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.63
Source: Homo sapiens
Molecule: cDNA FLJ50577, highly similar to Discs large homolog 4
UniProt: B7Z4H2
Pockets: 3 · best druggability 0.34

Structure

x-ray diffraction · resolution 1.63 · 2 distinct chains · 21% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	cDNA FLJ50577, highly similar to Discs large homolog 4	protein	101	21% helix, 35% strand	B7Z4H2
B	cDNA FLJ50577, highly similar to Discs large homolog 4	protein	102	22% helix, 38% strand	B7Z4H2

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.34	0.75	18	empty
2	72	0.32	0.74	12	empty
3	59	0.30	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 595 Å² buried · 12 hydrogen bonds · protein-protein

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 B7Z4H2
Elsewhere: RCSB PDB 8AH6 · PDBe 8AH6 · UniProt B7Z4H2

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