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Aedes aegypti kynurenine aminotrasferase

Analyse Aedes aegypti kynurenine aminotrasferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YIZ
Type: protein
Length: 836 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kynurenine aminotransferase
EC: 2.6.1.7, 2.6.1.64
UniProt: Q95VY4
Ligands: BR
Pockets: 11 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Kynurenine aminotransferase (EC 2.6.1.7, 2.6.1.64)	protein	418	44% helix, 15% strand	Q95VY4

Ligands and binding sites

BR · Bromide ion · ion · 5 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	327	0.73	0.85	48	empty
2	397	0.67	0.80	63	empty
3	54	0.61	0.92	15	empty
4	212	0.59	0.80	24	empty
5	136	0.51	0.80	24	empty

Interfaces

1 interface between chains.

A–B · 3062 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

1YIZ · Aedes aegypti kynurenine aminotrasferase · 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 Q95VY4
Elsewhere: RCSB PDB 1YIZ · PDBe 1YIZ · UniProt Q95VY4

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