Research workbench

Crystal structure of the complex of DPR6 domain 1 bound to dip-alpha domain 1+2

Analyse Crystal structure of the complex of DPR6 domain 1 bound to dip-alpha domain 1+2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EO9
Type: protein
Length: 312 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DPR6, isoform C; CG32791, isoform a
UniProt: M9PC40, Q9W4R3
Ligands: NAG, SO4

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DPR6, isoform C	protein	107	6% helix, 50% strand	M9PC40
B	CG32791, isoform a	protein	205	3% helix, 57% strand	Q9W4R3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
SO4 · Sulfate ion · ion · 4 copies · 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 · 961 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

5EO9 · Crystal Structure of the complex of Dpr6 Domain 1 bound to DIP-alpha Domain 1+2 · the same entry in another collection · chain A against A, TM-score 1.00

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 M9PC40
Every structure of UniProt Q9W4R3
Elsewhere: RCSB PDB 5EO9 · PDBe 5EO9 · UniProt M9PC40 · UniProt Q9W4R3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.