Research workbench

Crystal structure of the R132K:R111L:L121E mutant of cellular retinoic acid binding protein type II in complex with all-trans-retinal at 1.18 ångströms resolution

Analyse Crystal structure of the R132K:R111L:L121E mutant of cellular retinoic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2G7B
Type: protein
Length: 137 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular retinoic acid-binding protein 2
UniProt: P29373
Ligands: AZE, NA
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular retinoic acid-binding protein 2	protein	137	13% helix, 56% strand	P29373

Ligands and binding sites

AZE · All-trans axerophthene · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	286	0.76	0.88	45	AZE

Modifications

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

Compared structures

2G7B · Crystal Structure of the R132K:R111L:L121E mutant of Cellular Retinoic Acid Binding… · the same entry in another collection · chain A against A, TM-score 1.00

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 P29373
Elsewhere: RCSB PDB 2G7B · PDBe 2G7B · UniProt P29373

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