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Crystal structure of human cellular retinol binding protein 1 in complex with retinylamine

Analyse Crystal structure of human cellular retinol binding protein 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HA1
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Retinol-binding protein 1
UniProt: P09455
Ligands: RNE
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Retinol-binding protein 1	protein	140	10% helix, 53% strand	P09455

Ligands and binding sites

RNE · (2~{E},4~{E},6~{E},8~{E})-3,7-dimethyl-9-(2,6,6-trimethylcyclohexen-1-yl)nona-2,4,6,8-tetraen-1-amine · ligand · 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	256	0.83	0.94	38	RNE

Compared structures

5HA1 · Crystal structure of human cellular retinol binding protein 1 in complex with retinylamine · the same entry in another collection · chain A against A, TM-score 1.00
P09455 · AlphaFold monomer V2.0 prediction for retinol-binding protein 1 (P09455) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P09455
Elsewhere: RCSB PDB 5HA1 · PDBe 5HA1 · UniProt P09455

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