Research workbench

GID4 in complex with a peptide

Analyse GID4 in complex with a peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CD9
Type: protein
Length: 170 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-induced degradation protein 4 homolog; Tetrapeptide psrw
UniProt: Q8IVV7
Ligands: UNX
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-induced degradation protein 4 homolog	protein	166	11% helix, 45% strand	Q8IVV7
B	Tetrapeptide psrw	protein	4	0% helix, 50% strand	—

Ligands and binding sites

UNX · Unknown atom or ion · ion · 46 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	136	0.46	0.77	24	UNX

Interfaces

1 interface between chains.

A–B · 471 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

6CD9 · GID4 in complex with a peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q8IVV7 · AlphaFold monomer V2.0 prediction for glucose-induced degradation protein 4 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q8IVV7
Elsewhere: RCSB PDB 6CD9 · PDBe 6CD9 · UniProt Q8IVV7

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