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Human cRBP IV

Analyse Human cRBP IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LPJ
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Homo sapiens
Molecule: Retinol-binding protein IV, cellular
UniProt: Q96R05
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 11% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Retinol-binding protein IV, cellular	protein	133	11% helix, 56% strand	Q96R05

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	352	0.80	0.89	43	empty

Compared structures

1LPJ · Human crbp IV · the same entry in another collection · chain A against A, TM-score 1.00
Q96R05 · AlphaFold monomer V2.0 prediction for retinoid-binding protein 7 (Q96R05) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q96R05
Elsewhere: RCSB PDB 1LPJ · PDBe 1LPJ · UniProt Q96R05

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