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Crystal structure of human nectin-like 5 full ectodomain (D1-D3)

Analyse Crystal structure of human nectin-like 5 full ectodomain (D1-D3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FQP
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Poliovirus receptor
UniProt: P15151
Ligands: NAG, BMA, FUC, MAN

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poliovirus receptor	protein	306	2% helix, 53% strand	P15151

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A
BMA · beta-D-mannopyranose · sugar · 4 copies
FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
MAN · alpha-D-mannopyranose · sugar

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 7 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

4FQP · Crystal structure of human Nectin-like 5 full ectodomain (D1-D3) · the same entry in another collection · chain A against A, TM-score 1.00
P15151 · AlphaFold monomer V2.0 prediction for poliovirus receptor (P15151) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P15151
Elsewhere: RCSB PDB 4FQP · PDBe 4FQP · UniProt P15151

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