MolNFT v1 · #86422 · protein

A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP(H)

4B65 · L-ornithine N5 monooxygenase: “A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP(H)”. X-ray diffraction, 3 ligands (FAD, NDP, SO4), 6 pockets (best druggability 0.82). MolNFT v1 #86422 on GenesisL1: 3D…

PDB: 4B65
Type: protein
Length: 456 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-ornithine N5 monooxygenase
UniProt: Q5SE95
Ligands: FAD, NDP, SO4
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-ornithine N5 monooxygenase	protein	456	34% helix, 21% strand	Q5SE95

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

6 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	1117	0.82	0.83	87	FAD, NDP, GOL
2	100	0.42	0.78	16	empty
3	103	0.38	0.75	17	GOL
4	73	0.37	0.77	20	empty
5	79	0.33	0.74	15	empty

Compared structures

4B65 · A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP(H) · 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 Q5SE95
Elsewhere: RCSB PDB 4B65 · PDBe 4B65 · UniProt Q5SE95

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