MolNFT v1 · #66973 · protein

Structure of the binary complex leucoanthocyanidin reductase - NADPH from vitis vinifera

3I6I · Putative leucoanthocyanidin reductase 1: “Structure of the binary complex leucoanthocyanidin reductase - NADPH from vitis vinifera”. X-ray diffraction, 1 ligand (NDP), 2 pockets (best druggability 0.72). MolNFT v1 #66973 on…

PDB: 3I6I
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative leucoanthocyanidin reductase 1
EC: 1.17.1.3
UniProt: Q4W2K4
Ligands: NDP
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative leucoanthocyanidin reductase 1 (EC 1.17.1.3)	protein	302	43% helix, 16% strand	Q4W2K4

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
ACY · Acetic acid · additive · chains A

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

Pockets

2 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	501	0.72	0.81	38	NDP, ACY
2	140	0.48	0.78	23	NDP

Compared structures

3I6I · Structure of the binary complex leucoanthocyanidin reductase - NADPH from vitis vinifera · 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 Q4W2K4
Elsewhere: RCSB PDB 3I6I · PDBe 3I6I · UniProt Q4W2K4

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