Research workbench

Crystal structure of PDZ1-2 from psd-95 with peptide ligand sequence rresei bound to both domains

Analyse Crystal structure of PDZ1-2 from psd-95 with peptide ligand sequence rresei… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SPZ
Type: protein
Length: 201 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disks large homolog 4; Arg-arg-glu-ser-glu-ile
UniProt: P78352
Ligands: GSH

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Disks large homolog 4	protein	189	15% helix, 40% strand	P78352
P, Q	Arg-arg-glu-ser-glu-ile	protein	6	0% helix, 50% strand	—

Ligands and binding sites

GSH · Glutathione · ligand · chains A

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

Interfaces

2 interfaces between chains.

A–Q · 514 Å² buried · 12 hydrogen bonds · protein-protein
A–P · 488 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6SPZ · Crystal structure of PDZ1-2 from PSD-95 with peptide ligand sequence RRESEI bound to both… · the same entry in another collection · chain A against A, TM-score 1.00
P78352 · AlphaFold monomer V2.0 prediction for disks large homolog 4 (P78352) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 P78352
Elsewhere: RCSB PDB 6SPZ · PDBe 6SPZ · UniProt P78352

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