MolNFT v1 · #102360 · protein

Crystal structure of a C-terminally truncated trimeric ectodomain of the C. elegans fusion protein eff-1

4OJE · Eff-1A: “Crystal structure of a C-terminally truncated trimeric ectodomain of the C. elegans fusion protein eff-1”. X-ray diffraction, 2 ligands (NAG, PO4), 3 pockets (best druggability 0.63). MolNFT v1 #102360 on GenesisL1: 3D…

PDB: 4OJE
Type: protein
Length: 457 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eff-1A
UniProt: G5ECA1
Ligands: NAG, PO4
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Eff-1A	protein	457	4% helix, 51% strand	G5ECA1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains H
PO4 · Phosphate ion · ion · 4 copies · 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	451	0.63	0.76	60	empty
2	71	0.37	0.78	17	empty
3	98	0.34	0.73	19	empty

Modifications

Observed in the structure: 7 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

4OJE · 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 4OJE · PDBe 4OJE · UniProt G5ECA1

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