MolNFT v1 · #138532 · protein

Crystal structure of cahj in complex with 5-methylsalicyl adenylate

5WM5 · Salicylate-AMP ligase: “Crystal structure of cahj in complex with 5-methylsalicyl adenylate”. X-ray diffraction, 1 ligand (B5Y), 3 pockets (best druggability 0.79). MolNFT v1 #138532 on GenesisL1: 3D structure, binding sites and…

PDB: 5WM5
Type: protein
Length: 533 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Salicylate-AMP ligase
UniProt: A0A140DJY3
Ligands: B5Y
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Salicylate-AMP ligase	protein	533	32% helix, 27% strand	A0A140DJY3

Ligands and binding sites

B5Y · 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine · ligand · chains A
ACT · Acetate ion · additive · 2 copies · chains A
GOL · Glycerol · additive · 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	549	0.79	0.85	71	B5Y, GOL
2	280	0.56	0.76	29	empty
3	52	0.45	0.84	20	empty

Compared structures

5WM5 · Crystal Structure of CahJ in Complex with 5-Methylsalicyl Adenylate · 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 A0A140DJY3
Elsewhere: RCSB PDB 5WM5 · PDBe 5WM5 · UniProt A0A140DJY3

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