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Kuenenia stuttgartiensis hydroxylamine oxidoreductase

Analyse Kuenenia stuttgartiensis hydroxylamine oxidoreductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N4J
Type: protein
Length: 497 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxylamine oxidoreductase
EC: 1.7.3.4
UniProt: Q1PX48
Ligands: HEC, HG1, PO4
Pockets: 4 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxylamine oxidoreductase (EC 1.7.3.4)	protein	497	48% helix, 3% strand	Q1PX48

Ligands and binding sites

HEC · Heme C · ligand · 8 copies · chains A
HG1 · 1-[(4-cyclohexylbutanoyl)(2-hydroxyethyl)amino]-1-deoxy-D-glucitol · ligand · 4 copies · 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

4 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	1075	0.89	0.91	124	HEC
2	51	0.54	0.89	16	empty
3	72	0.47	0.83	15	empty
4	79	0.34	0.75	19	empty

Modifications

Observed in the structure: 16 cofactor (heme c attachment).

Compared structures

4N4J · Kuenenia stuttgartiensis hydroxylamine oxidoreductase · 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 Q1PX48
Elsewhere: RCSB PDB 4N4J · PDBe 4N4J · UniProt Q1PX48

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