MolNFT v1 · #24319 · protein

N-terminal domain of sialoadhesin (mouse) in complex with glycopeptide

1URL: “N-terminal domain of sialoadhesin (mouse) in complex with glycopeptide”. X-ray diffraction, 1 ligand (SIA). MolNFT v1 #24319 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1URL
Type: protein
Length: 124 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sialoadhesin; Ala-gly-his-thr-TRP-gly-hia
UniProt: Q62230
Ligands: SIA

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sialoadhesin	protein	118	5% helix, 46% strand	Q62230
B	Ala-gly-his-thr-TRP-gly-hia	protein	6	0% helix, 0% strand	—

Ligands and binding sites

SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A, B

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

Interfaces

1 interface between chains.

A–B · 205 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide, 1 glycan, 1 modified (disulfide, O-glycosylation, nonstandard).

Compared structures

1URL · N-terminal domain of sialoadhesin (mouse) in complex with glycopeptide · the same entry in another collection · chain A against A, TM-score 1.00
Q62230 · AlphaFold monomer V2.0 prediction for sialoadhesin (Q62230) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q62230
Elsewhere: RCSB PDB 1URL · PDBe 1URL · UniProt Q62230

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