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Crystal structure of the FAD dependent oxidoreductase PA4991 from pseudomonas aeruginosa

Analyse Crystal structure of the FAD dependent oxidoreductase PA4991 from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EZ7
Type: protein
Length: 363 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flavoenzyme PA4991
UniProt: Q9HUH4
Ligands: FAD, HG
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flavoenzyme PA4991	protein	363	28% helix, 29% strand	Q9HUH4

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
HG · Mercury (II) ion · metal · 2 copies · 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	683	0.76	0.82	73	FAD
2	72	0.39	0.78	19	empty

Compared structures

5EZ7 · Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
Q9HUH4 · AlphaFold monomer V2.0 prediction for probable FAD-dependent oxidoreductase PA4991… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9HUH4
Elsewhere: RCSB PDB 5EZ7 · PDBe 5EZ7 · UniProt Q9HUH4

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