MolNFT v1 · #102358 · protein

Crystal structure of the wild-type full-length trimeric ectodomain of the C. elegans fusion protein eff-1

4OJC · Eff-1A: “Crystal structure of the wild-type full-length trimeric ectodomain of the C. elegans fusion protein eff-1”. X-ray diffraction, 2 ligands (NAG, SO4), 3 pockets (best druggability 0.58). MolNFT v1 #102358 on GenesisL1: 3D…

PDB: 4OJC
Type: protein
Length: 461 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eff-1A
UniProt: G5ECA1
Ligands: NAG, SO4
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eff-1A	protein	461	3% helix, 48% strand	G5ECA1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
SO4 · Sulfate ion · ion · 9 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	390	0.58	0.75	49	empty
2	87	0.43	0.79	17	SO4
3	74	0.32	0.74	16	empty

Modifications

Observed in the structure: 7 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

4OJC · Crystal structure of the wild-type full-length trimeric ectodomain of the C. elegans… · 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 G5ECA1
Elsewhere: RCSB PDB 4OJC · PDBe 4OJC · UniProt G5ECA1

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