Research workbench

T166A mutant of D-serine deaminase from salmonella typhimurium

Analyse T166A mutant of D-serine deaminase from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AA9
Type: protein
Length: 417 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-serine dehydratase
EC: 4.3.1.18
UniProt: Q8ZL08
Ligands: NA, PO4
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-serine dehydratase (EC 4.3.1.18)	protein	417	51% helix, 15% strand	Q8ZL08

Ligands and binding sites

NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · 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	193	0.55	0.79	32	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

6AA9 · T166A mutant of D-Serine deaminase from Salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
Q8ZL08 · AlphaFold monomer V2.0 prediction for D-serine dehydratase (Q8ZL08) · 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 Q8ZL08
Elsewhere: RCSB PDB 6AA9 · PDBe 6AA9 · UniProt Q8ZL08

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.