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Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis in the holo form obtained at pH 7.0

Analyse Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8YRT
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Haliscomenobacter hydrossis DSM 1100
Molecule: Aminotransferase class IV
UniProt: F4KWH0
Ligands: PLP
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 30% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase class IV	protein	282	30% helix, 30% strand	F4KWH0

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	312	0.64	0.80	52	PLP

Modifications

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

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 F4KWH0
Elsewhere: RCSB PDB 8YRT · PDBe 8YRT · UniProt F4KWH0

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