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The crystal structures of holo-and apo-cellular retinol binding protein II

Analyse The crystal structures of holo-and apo-cellular retinol binding protein II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OPA
Type: protein
Length: 266 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular retinol binding protein II
UniProt: P06768
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellular retinol binding protein II	protein	133	11% helix, 56% strand	P06768

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	303	0.84	0.95	34	empty
2	298	0.84	0.94	36	empty
3	103	0.37	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 390 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1OPA · The crystal structures of holo-and apo-cellular retinol binding protein II · the same entry in another collection · chain A against A, TM-score 1.00
P06768 · AlphaFold monomer V2.0 prediction for retinol-binding protein 2 (P06768) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P06768
Elsewhere: RCSB PDB 1OPA · PDBe 1OPA · UniProt P06768

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