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A. fumigatus ornithine hydroxylase (sida) bound to ornithine

Analyse A. fumigatus ornithine hydroxylase (sida) bound to ornithine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B69
Type: protein
Length: 448 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-ornithine N5 monooxygenase
UniProt: Q5SE95
Ligands: FAD, ORN, SO4
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-ornithine N5 monooxygenase	protein	448	35% helix, 22% strand	Q5SE95

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
ORN · L-ornithine · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1067	0.82	0.83	87	FAD, ORN
2	111	0.42	0.77	23	empty
3	73	0.40	0.79	17	empty
4	97	0.36	0.75	20	empty
5	80	0.34	0.74	14	GOL

Compared structures

4B69 · A. fumigatus ornithine hydroxylase (SidA) bound to ornithine · 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 4B69 · PDBe 4B69 · UniProt Q5SE95

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