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PDZ domain from rat SHANK3 bound to the C terminus of gkap

Analyse PDZ domain from rat SHANK3 bound to the C terminus of gkap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OVC
Type: protein
Length: 102 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SH3 and multiple ankyrin repeat domains protein 3; Gkap C terminus, synthetic peptide
UniProt: Q9JLU4
Ligands: ACE, CL

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SH3 and multiple ankyrin repeat domains protein 3	protein	96	18% helix, 35% strand	Q9JLU4
B	Gkap C terminus, synthetic peptide	protein	6	0% helix, 67% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, B
CL · Chloride ion · ion · chains A

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

Interfaces

1 interface between chains.

A–B · 562 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5OVC · PDZ domain from rat Shank3 bound to the C terminus of GKAP · the same entry in another collection · chain A against A, TM-score 1.00
Q9JLU4 · AlphaFold monomer V2.0 prediction for SH3 and multiple ankyrin repeat domains protein 3… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9JLU4
Elsewhere: RCSB PDB 5OVC · PDBe 5OVC · UniProt Q9JLU4

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