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Crystal structure of the glycopeptide N-methyltransferase mtfa complexed with sinefungin

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: 3G2Q
Type: protein
Length: 477 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PCZA361.24
UniProt: O52805
Ligands: SFG
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PCZA361.24	protein	247	27% helix, 34% strand	O52805
B	PCZA361.24	protein	230	27% helix, 35% strand	O52805

Ligands and binding sites

SFG · Sinefungin · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	639	0.66	0.76	78	SFG
2	564	0.66	0.76	59	SFG
3	247	0.56	0.78	33	empty
4	100	0.40	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 1648 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

3G2Q · Crystal Structure of the Glycopeptide N-methyltransferase MtfA complexed with sinefungin · the same entry in another collection · chain B against B, 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 3G2Q · PDBe 3G2Q · UniProt O52805

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