MolNFT v1 · #147200 · protein

Crystal structure of the apo domain-swapped dimer Q108K:T51D:A28H mutant of human cellular retinol binding protein II

6E5Q · Retinol-binding protein 2: “Crystal structure of the apo domain-swapped dimer Q108K:T51D:A28H mutant of human cellular retinol binding…”. X-ray diffraction, 1 pocket (best druggability 0.51). MolNFT v1 #147200 on GenesisL1: 3D…

PDB: 6E5Q
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Retinol-binding protein 2
UniProt: P50120
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Retinol-binding protein 2	protein	133	11% helix, 49% strand	P50120

Ligands and binding sites

ACT · Acetate ion · additive · 4 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	213	0.51	0.76	28	empty

Compared structures

6E5Q · Crystal structure of the apo domain-swapped dimer Q108K:T51D:A28H mutant of human… · the same entry in another collection · chain A against A, TM-score 1.00
P50120 · AlphaFold monomer V2.0 prediction for retinol-binding protein 2 (P50120) · a predicted model of the same protein · chain A against A, TM-score 0.57

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 P50120
Elsewhere: RCSB PDB 6E5Q · PDBe 6E5Q · UniProt P50120

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