MolNFT v1 · #70551 · protein

The crystal structure of fatty acyl-adenylate ligase from L. pneumophila in complex with acyl adenylate and pyrophosphate

3LNV · Saframycin MX1 synthetase B: “The crystal structure of fatty acyl-adenylate ligase from L. pneumophila in complex with acyl adenylate and…”. X-ray diffraction, 2 ligands (1ZZ, POP), 4 pockets (best druggability 0.88). MolNFT v1…

PDB: 3LNV
Type: protein
Length: 566 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saframycin MX1 synthetase B
UniProt: Q5ZTD3
Ligands: 1ZZ, POP
Pockets: 4 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saframycin MX1 synthetase B	protein	566	37% helix, 26% strand	Q5ZTD3

Ligands and binding sites

1ZZ · 5'-O-[(S)-(dodecanoyloxy)(hydroxy)phosphoryl]adenosine · ligand · chains A
POP · Pyrophosphate 2- · ligand · chains A

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

Pockets

4 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	1074	0.88	0.89	111	1ZZ, POP
2	364	0.60	0.76	49	empty
3	59	0.33	0.77	12	empty
4	54	0.29	0.74	13	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

3LNV · The crystal structure of fatty acyl-adenylate ligase from L. pneumophila in complex with… · 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 Q5ZTD3
Elsewhere: RCSB PDB 3LNV · PDBe 3LNV · UniProt Q5ZTD3

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