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

Analyse Crystal structure of the plantazolicin methyltransferase bpuml 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: 5DM1
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyltransferase domain family
UniProt: B4ADV2
Ligands: 5D7, SAH
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyltransferase domain family	protein	257	53% helix, 20% strand	B4ADV2

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
GOL · Glycerol · additive · 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	490	0.78	0.86	71	5D7, SAH, GOL

Compared structures

5DM1 · Crystal structure of the plantazolicin methyltransferase BpumL 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 B4ADV2
Elsewhere: RCSB PDB 5DM1 · PDBe 5DM1 · UniProt B4ADV2

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