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Structural studies on corn nitrate reductase: refined structure of the cytochrome B reductase fragment at 2.5 ångströms, its ADP complex and an active site mutant and modeling of the cytochrome B domain

Analyse Structural studies on corn nitrate reductase: refined structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CND
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH-dependent nitrate reductase
EC: 1.6.6.1
UniProt: P17571
Ligands: FAD
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH-dependent nitrate reductase (EC 1.6.6.1)	protein	260	25% helix, 35% strand	P17571

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

3 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	463	0.63	0.76	53	FAD
2	70	0.58	0.89	23	empty
3	74	0.30	0.73	24	empty

Compared structures

2CND · Structural studies on corn nitrate reductase: refined structure of the cytochrome B… · the same entry in another collection · chain A against A, TM-score 1.00
P17571 · AlphaFold monomer V2.0 prediction for nitrate reductase [NADH] (P17571) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P17571
Elsewhere: RCSB PDB 2CND · PDBe 2CND · UniProt P17571

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