MolNFT v1 · #68788 · protein

Crystal structure of the dehydrogenase part of multifuctional enzyme 1 from C.ELEGANS

3K6J · Protein F01G10.3, confirmed by transcript evidence: “Crystal structure of the dehydrogenase part of multifuctional enzyme 1 from C.ELEGANS”. X-ray diffraction, 2 ligands (ZN, PO4), 7 pockets (best druggability 0.49). MolNFT v1…

PDB: 3K6J
Type: protein
Length: 430 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein F01G10.3, confirmed by transcript evidence
UniProt: O17762
Ligands: ZN, PO4
Pockets: 7 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein F01G10.3, confirmed by transcript evidence	protein	430	48% helix, 12% strand	O17762

Ligands and binding sites

ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 4 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.49	0.82	15	empty
2	201	0.49	0.76	33	PO4
3	118	0.48	0.80	20	PO4
4	125	0.43	0.76	29	empty
5	56	0.34	0.78	18	empty

Compared structures

3K6J · Crystal structure of the dehydrogenase part of multifuctional enzyme 1 from 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 O17762
Elsewhere: RCSB PDB 3K6J · PDBe 3K6J · UniProt O17762

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