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Crystal structure of the glycopeptide N-methyltransferase mtfa complexed with (S)-adenosyl-L-methionine (SAM)

Analyse Crystal structure of the glycopeptide N-methyltransferase mtfa complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3G2O
Type
protein
Length
472 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PCZA361.24
UniProt
O52805
Ligands
SAM
Pockets
6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APCZA361.24protein24430% helix, 34% strandO52805
BPCZA361.24protein22827% helix, 35% strandO52805

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17630.720.78104SAM
22040.560.8028empty
3930.370.7615empty
4690.370.7721empty
5760.360.7619empty

Interfaces

1 interface between chains.

  • A–B · 1623 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 3G2O · Crystal Structure of the Glycopeptide N-methyltransferase MtfA complexed with… · the same entry in another collection · chain B against B, TM-score 1.00

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