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Crystal structure of E-selectin LECTIN/EGF domains complexed with slex

Analyse Crystal structure of E-selectin LECTIN/EGF domains complexed with slex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G1T
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E-selectin
UniProt: P16581
Ligands: MAG, GAL, SIA, FUC, CA

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E-selectin	protein	157	16% helix, 32% strand	P16581

Ligands and binding sites

MAG · methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside · sugar
GAL · beta-D-galactopyranose · sugar · chains A
SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A
FUC · alpha-L-fucopyranose · sugar · chains A
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 (disulfide).

Compared structures

1G1T · Crystal structure of E-selectin LECTIN/EGF domains complexed with slex · the same entry in another collection · chain A against A, TM-score 1.00
P16581 · AlphaFold monomer V2.0 prediction for E-selectin (P16581) · 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 P16581
Elsewhere: RCSB PDB 1G1T · PDBe 1G1T · UniProt P16581

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