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M2 mutant (R111K:Y134F:T54V:R132Q:P39Y:R59Y) of human cellular retinoic acid binding protein II - 6 conjugate

Analyse M2 mutant (R111K:Y134F:T54V:R132Q:P39Y:R59Y) of human 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: 6ZSW
Type: protein
Length: 138 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: QPB
Pockets: 1 · best druggability 0.72

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	138	13% helix, 54% strand	P29373

Ligands and binding sites

QPB · methyl (~{Z})-3-(4-hydroxyphenyl)-2-methyl-prop-2-enoate · ligand · chains A
ACT · Acetate ion · additive · 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	386	0.72	0.83	39	QPB

Modifications

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

Compared structures

6ZSW · M2 mutant (R111K:Y134F:T54V:R132Q:P39Y:R59Y) of human 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 6ZSW · PDBe 6ZSW · UniProt P29373

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