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Crystal structure of the all-trans retinal-bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E:I63D mutant of human cellular retinoic acid binding protein II in the dark at 1.97 ångström resolution

Analyse Crystal structure of the all-trans retinal-bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6NOE
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
RET
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACellular retinoic acid-binding protein 2protein13713% helix, 53% strandP29373

Ligands and binding sites

  • RET · Retinal · ligand · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14270.730.8338RET

Modifications

Observed in the structure: 1 cofactor (retinal Schiff base).

Compared structures

  • 6NOE · Crystal Structure of the All-Trans Retinal-Bound… · the same entry in another collection · chain A against A, TM-score 1.00

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