Research workbench

CTBP1/BARS GLY172->glu mutant structure: impairing NAD(H) binding and dimerization

Analyse CTBP1/BARS GLY172->glu mutant structure: impairing NAD(H) binding and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GA0
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-terminal-binding protein 1
EC: 1.1.1.-
UniProt: Q9Z2F5
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-terminal-binding protein 1 (EC 1.1.1.-)	protein	337	35% helix, 15% strand	Q9Z2F5

Ligands and binding sites

FMT · Formic acid · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	532	0.75	0.83	58	FMT
2	97	0.38	0.76	20	empty

Compared structures

3GA0 · CtBP1/BARS Gly172->Glu mutant structure: impairing NAD(H) binding and dimerization · the same entry in another collection · chain A against A, TM-score 1.00
Q9Z2F5 · AlphaFold monomer V2.0 prediction for C-terminal-binding protein 1 (Q9Z2F5) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9Z2F5
Elsewhere: RCSB PDB 3GA0 · PDBe 3GA0 · UniProt Q9Z2F5

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