MolNFT v1 · #64418 · protein

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

3G2P · PCZA361.24: “Crystal structure of the glycopeptide N-methyltransferase mtfa complexed with (S)-adenosyl-L-homocysteine…”. X-ray diffraction, 1 ligand (SAH), 4 pockets (best druggability 0.70). MolNFT v1 #64418 on GenesisL1: 3D…

PDB: 3G2P
Type: protein
Length: 488 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PCZA361.24
UniProt: O52805
Ligands: SAH
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PCZA361.24	protein	251	29% helix, 33% strand	O52805
B	PCZA361.24	protein	237	29% helix, 31% strand	O52805

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	772	0.70	0.76	94	SAH
2	658	0.66	0.75	69	SAH
3	71	0.31	0.74	22	empty
4	64	0.30	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1691 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

3G2P · Crystal Structure of the Glycopeptide N-methyltransferase MtfA complexed with… · 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 O52805
Elsewhere: RCSB PDB 3G2P · PDBe 3G2P · UniProt O52805

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