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Helicobacter pylori psec, aminotransferase involved in the biosynthesis of pseudoaminic acid

Analyse Helicobacter pylori psec, aminotransferase involved in the biosynthesis of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FN6
Type: protein
Length: 743 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase
Ligands: PO4
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase	protein	372	42% helix, 18% strand	—
B	Aminotransferase	protein	371	41% helix, 18% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

5 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	685	0.76	0.82	63	PO4
2	720	0.75	0.80	72	PO4
3	120	0.42	0.76	22	empty
4	68	0.37	0.77	10	empty
5	78	0.31	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 2812 Å² buried · 44 hydrogen bonds · protein-protein

Compared structures

2FN6 · Helicobacter pylori PseC, aminotransferase involved in the biosynthesis of pseudoaminic… · 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
Elsewhere: RCSB PDB 2FN6 · PDBe 2FN6

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