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Crystal structure of the 13-cis product of all-trans retinal-bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E mutant of human cellular retinoic acid binding protein II irradiated with 400 nm laser (30 seconds) at 1.9 ångström

Analyse Crystal structure of the 13-cis product of 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: 6MQY
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, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular retinoic acid-binding protein 2	protein	137	13% helix, 54% strand	P29373

Ligands and binding sites

RET · Retinal · ligand · chains A
GOL · Glycerol · additive · 3 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	425	0.73	0.83	41	RET

Modifications

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

Compared structures

6MQY · Crystal Structure of the 13-cis Product of All-trans Retinal-Bound… · 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 6MQY · PDBe 6MQY · UniProt P29373

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