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Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility

Analyse Two homologous rat cellular retinol-binding proteins differ in local structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MX8
Type: protein
Length: 134 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular retinol-binding protein I, holo
UniProt: P02696
Ligands: RTL
Pockets: 2 · best druggability 0.85

Structure

solution nmr · 1 distinct chain · 10% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular retinol-binding protein I, holo	protein	134	10% helix, 42% strand	P02696

Ligands and binding sites

RTL · Retinol · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	635	0.85	0.89	53	RTL
2	50	0.28	0.75	14	empty

Compared structures

1MX8 · Two homologous rat cellular retinol-binding proteins differ in local structure and… · the same entry in another collection · chain A against A, TM-score 1.00
P02696 · AlphaFold monomer V2.0 prediction for retinol-binding protein 1 (P02696) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P02696
Elsewhere: RCSB PDB 1MX8 · PDBe 1MX8 · UniProt P02696

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