MolNFT v1 · #118028 · protein

Structure at 1.75 a resolution of a glycosylated, lipid-binding, lipocalin-like protein

5EPQ · Milk protein: “Structure at 1.75 a resolution of a glycosylated, lipid-binding, lipocalin-like protein”. X-ray diffraction, 3 ligands (OLA, NAG, BMA), 2 pockets (best druggability 0.67). MolNFT v1 #118028 on GenesisL1: 3D structure…

PDB: 5EPQ
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Milk protein
UniProt: Q6SVB6
Ligands: OLA, NAG, BMA
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Milk protein	protein	153	10% helix, 45% strand	Q6SVB6

Ligands and binding sites

OLA · Oleic acid · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
BMA · beta-D-mannopyranose · sugar · 2 copies
EDO · 1,2-ethanediol · additive · 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	153	0.67	0.87	25	OLA
2	55	0.33	0.77	12	empty

Modifications

Observed in the structure: 4 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

5EPQ · Structure at 1.75 A resolution of a glycosylated, lipid-binding, lipocalin-like protein · the same entry in another collection · chain A against A, TM-score 1.00

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 Q6SVB6
Elsewhere: RCSB PDB 5EPQ · PDBe 5EPQ · UniProt Q6SVB6

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