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Crystal structure of the plantazolicin methyltransferase baml in complex with monoazolic desmethylpzn analog and sah

Analyse Crystal structure of the plantazolicin methyltransferase baml in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DLY
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plantazolicin methyltransferase baml
UniProt: A7Z2A9
Ligands: 5D7, SAH
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plantazolicin methyltransferase baml	protein	266	55% helix, 18% strand	A7Z2A9

Ligands and binding sites

5D7 · prop-2-en-1-yl 2-[(1S)-1-amino-4-carbamimidamidobutyl]-1,3-thiazole-4-carboxylate · ligand · chains A
SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	462	0.83	0.90	62	5D7, SAH

Compared structures

5DLY · Crystal structure of the plantazolicin methyltransferase BamL in complex with monoazolic… · 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 A7Z2A9
Elsewhere: RCSB PDB 5DLY · PDBe 5DLY · UniProt A7Z2A9

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