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Crystal structure of cahj in complex with 6-methylsalicyl adenylate

Analyse Crystal structure of cahj in complex with 6-methylsalicyl adenylate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WM4
Type: protein
Length: 534 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Salicylate-AMP ligase
UniProt: A0A140DJY3
Ligands: B5M, MG
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Salicylate-AMP ligase	protein	534	33% helix, 26% strand	A0A140DJY3

Ligands and binding sites

B5M · 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine · ligand · chains A
MG · Magnesium ion · metal · chains A
ACT · Acetate ion · additive · 6 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

2 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	859	0.79	0.82	92	B5M
2	52	0.48	0.86	21	empty

Compared structures

5WM4 · Crystal Structure of CahJ in Complex with 6-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 5WM4 · PDBe 5WM4 · UniProt A0A140DJY3

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