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Crystal structure of D-amino acid aminotrensferase from haliscomenobacter hydrossis complexed with D-cycloserine

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

PDB: 8AHU
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase class IV
UniProt: F4KWH0
Ligands: LCS
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase class IV	protein	283	30% helix, 29% strand	F4KWH0

Ligands and binding sites

LCS · [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate · ligand · chains A
GOL · Glycerol · additive · chains A

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

Pockets

3 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	213	0.66	0.85	40	LCS
2	80	0.36	0.76	15	empty
3	77	0.33	0.74	21	empty

Compared structures

8AHU · Crystal structure of D-amino acid aminotrensferase from Haliscomenobacter hydrossis… · the same entry in another collection · chain A against A, TM-score 1.00

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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 8AHU · PDBe 8AHU · UniProt F4KWH0

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