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Crystal structure of icam-5 D1-D4 ectodomain fragment, space group P21

Analyse Crystal structure of icam-5 D1-D4 ectodomain fragment, space group P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OI9
Type: protein
Length: 378 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Intercellular adhesion molecule 5
UniProt: Q9UMF0
Ligands: NAG, BMA, MAN

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Intercellular adhesion molecule 5	protein	378	4% helix, 61% strand	Q9UMF0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A
BMA · beta-D-mannopyranose · sugar
MAN · alpha-D-mannopyranose · sugar
EDO · 1,2-ethanediol · additive · 31 copies · chains A

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

Modifications

Observed in the structure: 9 glycan, 5 disulfide (N-glycosylation, disulfide).

Compared structures

4OI9 · Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group P21 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UMF0 · AlphaFold monomer V2.0 prediction for intercellular adhesion molecule 5 (Q9UMF0) · 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 Q9UMF0
Elsewhere: RCSB PDB 4OI9 · PDBe 4OI9 · UniProt Q9UMF0

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