MolNFT v1 · #151481 · protein

Crystal structure of the O-methyltransferase from the trans-at pks multienzyme C0ZGQ3 of brevibacillus brevis in complex with S- adenosyl-L-homocysteine

6HP2 · Putative polyketide synthase: “Crystal structure of the O-methyltransferase from the trans-at pks multienzyme C0ZGQ3 of brevibacillus brevis…”. X-ray diffraction, 1 ligand (SAH), 3 pockets (best druggability 0.68). MolNFT v1 #151481…

PDB: 6HP2
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative polyketide synthase
UniProt: C0ZGQ3
Ligands: SAH
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative polyketide synthase	protein	297	43% helix, 21% strand	C0ZGQ3

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	396	0.68	0.81	49	SAH
2	63	0.40	0.80	11	empty
3	53	0.34	0.78	18	empty

Compared structures

6HP2 · Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of… · 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 C0ZGQ3
Elsewhere: RCSB PDB 6HP2 · PDBe 6HP2 · UniProt C0ZGQ3

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