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Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from ralstonia metallidurans

Analyse Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from ralstonia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YFU
Type: protein
Length: 174 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-hydroxyanthranilate-3,4-dioxygenase
EC: 1.13.11.6
Ligands: FE, CL
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-hydroxyanthranilate-3,4-dioxygenase (EC 1.13.11.6)	protein	174	15% helix, 37% strand	—

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	417	0.72	0.83	48	FE, CL
2	60	0.31	0.76	12	empty

Compared structures

1YFU · Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans · 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
Elsewhere: RCSB PDB 1YFU · PDBe 1YFU

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