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Crystal structure of the salicylate 1,2-dioxygenase from pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate

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

PDB: 4FAG
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gentisate 1,2-dioxygenase
EC: 1.13.11.4
UniProt: Q67FT0
Ligands: GTQ, FE
Pockets: 5 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gentisate 1,2-dioxygenase (EC 1.13.11.4)	protein	362	19% helix, 31% strand	Q67FT0

Ligands and binding sites

GTQ · 2,5-dihydroxybenzoic acid · ligand · chains A
FE · Fe (III) ion · metal · chains A
GOL · Glycerol · additive · 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	139	0.50	0.80	32	empty
2	185	0.45	0.74	23	empty
3	130	0.43	0.76	19	FE, GTQ
4	131	0.43	0.76	17	empty
5	132	0.43	0.76	26	empty

Compared structures

4FAG · Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter… · 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 Q67FT0
Elsewhere: RCSB PDB 4FAG · PDBe 4FAG · UniProt Q67FT0

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