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Crystal structure of S. aureus tars 1-349 in complex with udp-glcnac

Analyse Crystal structure of S. aureus tars 1-349 in complex with udp-glcnac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TZJ
Type: protein
Length: 698 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl transferase
EC: 2.4.1.-
UniProt: A0A181F8T0
Ligands: UD1
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A	Glycosyl transferase (EC 2.4.1.-)	protein	349	42% helix, 17% strand	A0A181F8T0

Ligands and binding sites

UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · 2 copies · chains C, A

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	601	0.73	0.81	48	UD1
2	552	0.73	0.82	53	UD1
3	127	0.39	0.74	24	empty
4	65	0.38	0.78	16	empty
5	67	0.35	0.77	14	empty

Interfaces

1 interface between chains.

C–A · 410 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5TZJ · Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc · the same entry in another collection · chain C against C, 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 A0A181F8T0
Elsewhere: RCSB PDB 5TZJ · PDBe 5TZJ · UniProt A0A181F8T0

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