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EGF domains 1,2,5 of human EMR2, a 7-tm immune system molecule, in complex with strontium.

Analyse EGF domains 1,2,5 of human EMR2, a 7-tm immune system molecule, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BOX
Type: protein
Length: 135 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: EGF-like module containing mucin-like hormone receptor-like 2 precursor
UniProt: Q9UHX3
Ligands: SR, CL

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	EGF-like module containing mucin-like hormone receptor-like 2 precursor	protein	135	7% helix, 32% strand	Q9UHX3

Ligands and binding sites

SR · Strontium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A
CAC · Cacodylate ion · additive · chains A

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

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

2BOX · EGF Domains 1,2,5 of human EMR2, a 7-TM immune system molecule, in complex with strontium. · the same entry in another collection · chain A against A, TM-score 1.00
Q9UHX3 · AlphaFold monomer V2.0 prediction for adhesion G protein-coupled receptor E2 (Q9UHX3) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 Q9UHX3
Elsewhere: RCSB PDB 2BOX · PDBe 2BOX · UniProt Q9UHX3

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