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Crystal structure of bovine holo-rbp at pH 2.0

Analyse Crystal structure of bovine holo-rbp at pH 2.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KT3
Type: protein
Length: 175 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasma retinol-binding protein
UniProt: P18902
Ligands: RTL
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plasma retinol-binding protein	protein	175	11% helix, 46% strand	P18902

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	288	0.82	0.93	31	RTL
2	105	0.42	0.77	16	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1KT3 · Crystal structure of bovine holo-RBP at pH 2.0 · the same entry in another collection · chain A against A, TM-score 1.00
P18902 · AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P18902) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P18902
Elsewhere: RCSB PDB 1KT3 · PDBe 1KT3 · UniProt P18902

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