Research workbench

NOROXOMARITIDINE/NORCRAUGSODINE reductase in complex with NADP+ and piperonal

Analyse NOROXOMARITIDINE/NORCRAUGSODINE reductase in complex with NADP+ and piperonal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FFF
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NOROXOMARITIDINE/NORCRAUGSODINE reductase
Ligands: NAP, 5XC
Pockets: 5 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	NOROXOMARITIDINE/NORCRAUGSODINE reductase	protein	257	52% helix, 16% strand	—

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
5XC · 1,3-benzodioxole-5-carbaldehyde · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.75	0.86	40	NAP
2	575	0.74	0.82	51	NAP, 5XC
3	78	0.41	0.79	21	empty
4	139	0.40	0.74	18	empty
5	77	0.36	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 1844 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5FFF · Noroxomaritidine/Norcraugsodine Reductase in complex with NADP+ and piperonal · 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
Elsewhere: RCSB PDB 5FFF · PDBe 5FFF

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