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The crystal structure of a possible phosphate ACETYL/BUTARYL transferase from listeria monocytogenes egd-E.

Analyse The crystal structure of a possible phosphate ACETYL/BUTARYL transferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TNG
Type: protein
Length: 287 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LMO1369 protein
UniProt: Q8Y7B7
Ligands: NI
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LMO1369 protein	protein	287	36% helix, 19% strand	Q8Y7B7

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 5 copies · 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	62	0.50	0.86	16	PEG
2	86	0.44	0.80	18	PEG
3	122	0.41	0.75	22	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3TNG · The crystal structure of a possible phosphate acetyl/butaryl transferase from Listeria… · 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 Q8Y7B7
Elsewhere: RCSB PDB 3TNG · PDBe 3TNG · UniProt Q8Y7B7

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