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The crystal structure of human kynurenine aminotransferase II

Analyse The crystal structure of human kynurenine aminotransferase II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EFS
Type: protein
Length: 425 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: KYNURENINE/ALPHA-aminoadipate aminotransferase, mitochondrial
EC: 2.6.1.39, 2.6.1.7
UniProt: Q8N5Z0
Pockets: 5 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	KYNURENINE/ALPHA-aminoadipate aminotransferase, mitochondrial (EC 2.6.1.39, 2.6.1.7)	protein	425	40% helix, 15% strand	Q8N5Z0

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	90	0.50	0.83	18	empty
2	75	0.43	0.81	22	empty
3	81	0.36	0.76	18	empty
4	64	0.35	0.77	13	empty
5	69	0.33	0.75	14	empty

Compared structures

5EFS · The crystal structure of human kynurenine aminotransferase II · the same entry in another collection · chain A against A, TM-score 1.00
Q8N5Z0 · AlphaFold monomer V2.0 prediction for KYNURENINE/ALPHA-aminoadipate aminotransferase… · 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 Q8N5Z0
Elsewhere: RCSB PDB 5EFS · PDBe 5EFS · UniProt Q8N5Z0

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