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Crystal structure of homo sapiens kynureninase

Analyse Crystal structure of homo sapiens kynureninase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HZP
Type: protein
Length: 447 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kynureninase
EC: 3.7.1.3
UniProt: Q16719
Ligands: PLP
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kynureninase (EC 3.7.1.3)	protein	447	45% helix, 15% strand	Q16719

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

4 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	50	0.51	0.88	23	PLP
2	154	0.43	0.74	24	empty
3	93	0.39	0.76	20	empty
4	79	0.38	0.78	23	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

2HZP · Crystal Structure of Homo Sapiens Kynureninase · the same entry in another collection · chain A against A, TM-score 1.00
Q16719 · AlphaFold monomer V2.0 prediction for kynureninase (Q16719) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q16719
Elsewhere: RCSB PDB 2HZP · PDBe 2HZP · UniProt Q16719

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