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Cryatal structure of hydroxyquinol 1,2-dioxygenase from pseudomonas putida dll-E4

Analyse Cryatal structure of hydroxyquinol 1,2-dioxygenase from pseudomonas putida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N9T
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pnpc
EC: 1.13.11.37
UniProt: C6FI44
Ligands: HGX, FE
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pnpc (EC 1.13.11.37)	protein	286	27% helix, 23% strand	C6FI44

Ligands and binding sites

HGX · 1-heptadecanoyl-2-tridecanoyl-3-glycerol-phosphonyl choline · ligand · chains A
FE · Fe (III) ion · metal · chains A
FLC · Citrate anion · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	173	0.59	0.82	26	FLC

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

3N9T · Cryatal structure of Hydroxyquinol 1,2-dioxygenase from Pseudomonas putida DLL-E4 · 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 C6FI44
Elsewhere: RCSB PDB 3N9T · PDBe 3N9T · UniProt C6FI44

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