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Elxo Y152F with NADPH bound

Analyse Elxo Y152F with NADPH bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QED
Type: protein
Length: 496 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elxo
UniProt: I6ZQW6
Ligands: NAP, SO4
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Elxo	protein	248	52% helix, 16% strand	I6ZQW6

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	705	0.74	0.80	45	NAP
2	714	0.74	0.79	47	NAP
3	145	0.52	0.80	23	empty
4	176	0.50	0.77	24	empty
5	87	0.38	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 1446 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4QED · ElxO Y152F with NADPH Bound · 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 I6ZQW6
Elsewhere: RCSB PDB 4QED · PDBe 4QED · UniProt I6ZQW6

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