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Co-crystal structure of P. aeruginosa lpxc-ACHN975 complex

Analyse Co-crystal structure of P. aeruginosa lpxc-ACHN975 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MOO
Type: protein
Length: 301 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-3-O-acyl-N-acetylglucosamine deacetylase
EC: 3.5.1.108
UniProt: A0A072ZC86
Ligands: A5F, ZN
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108)	protein	301	24% helix, 33% strand	A0A072ZC86

Ligands and binding sites

A5F · N-[(2S)-3-azanyl-3-methyl-1-(oxidanylamino)-1-oxidanylidene-butan-2-yl]-4-[4-[(1R,2R)-2-(hydroxymethyl)cyclopropyl]buta -1,3-diynyl]benzamide · ligand · chains A
ZN · Zinc ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	401	0.67	0.80	40	A5F
2	156	0.64	0.86	25	empty
3	55	0.38	0.80	19	empty

Compared structures

6MOO · Co-Crystal structure of P. aeruginosa LpxC-achn975 complex · 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 A0A072ZC86
Elsewhere: RCSB PDB 6MOO · PDBe 6MOO · UniProt A0A072ZC86

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