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L-selectin lectin and EGF domains

Analyse L-selectin lectin and EGF domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CFW
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Homo sapiens
Molecule: L-selectin
UniProt: P14151
Ligands: NAG, MAN, BMA, CA

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 15% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-selectin	protein	156	15% helix, 34% strand	P14151

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies
BMA · beta-D-mannopyranose · sugar
CA · Calcium ion · metal · chains A

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

Modifications

Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

3CFW · L-selectin lectin and EGF domains · the same entry in another collection · chain A against A, TM-score 1.00
P14151 · AlphaFold monomer V2.0 prediction for L-selectin (P14151) · 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 P14151
Elsewhere: RCSB PDB 3CFW · PDBe 3CFW · UniProt P14151

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