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Crystal structure of the apo R132K:Y134F:R111L:L121D mutant of cellular retinoic acid-binding protein II at 1.94 ångström resolution

Analyse Crystal structure of the apo R132K:Y134F:R111L:L121D mutant of cellular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FA9
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular retinoic acid-binding protein 2
UniProt: P29373
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellular retinoic acid-binding protein 2	protein	137	12% helix, 55% strand	P29373

Ligands and binding sites

ACT · Acetate ion · additive · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	533	0.76	0.83	46	empty
2	606	0.74	0.81	51	empty
3	185	0.44	0.73	24	ACT

Interfaces

1 interface between chains.

A–B · 637 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3FA9 · Crystal structure of the apo R132K:Y134F:R111L:L121D mutant of cellular retinoic… · 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 3FA9 · PDBe 3FA9 · UniProt P29373

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