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Crystal structure of a C-terminally truncated trimeric ectodomain of the C. elegans fusion protein eff-1 G260A/D321E/D322E mutant

Analyse Crystal structure of a C-terminally truncated trimeric ectodomain of the C.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OJD
Type: protein
Length: 444 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eff-1A
UniProt: G5ECA1
Ligands: NAG, BMA
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Eff-1A	protein	444	5% helix, 51% strand	G5ECA1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains H
BMA · beta-D-mannopyranose · sugar · chains H

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	350	0.57	0.75	47	empty
2	75	0.36	0.76	15	empty
3	62	0.29	0.74	18	empty

Modifications

Observed in the structure: 7 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

4OJD · Crystal structure of a C-terminally truncated trimeric ectodomain of the C. elegans… · the same entry in another collection · chain H against H, 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 4OJD · PDBe 4OJD · UniProt G5ECA1

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