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Crystal structure of T.TH HB8 glutamine aminotransferase

Analyse Crystal structure of T.TH HB8 glutamine aminotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V2D
Type: protein
Length: 365 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamine aminotransferase
EC: 2.6.1.15
UniProt: Q75WK2
Ligands: PLP
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamine aminotransferase (EC 2.6.1.15)	protein	365	44% helix, 18% strand	Q75WK2

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

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	191	0.56	0.79	30	PLP

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

1V2D · Crystal Structure of T.th HB8 Glutamine Aminotransferase · 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 Q75WK2
Elsewhere: RCSB PDB 1V2D · PDBe 1V2D · UniProt Q75WK2

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