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Crystal structure of a SAM dependent methyltransferase from archaeoglobus fulgidus

Analyse Crystal structure of a SAM dependent methyltransferase from archaeoglobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DLI
Type: protein
Length: 663 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyltransferase
UniProt: O30190
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Methyltransferase	protein	221	45% helix, 18% strand	O30190

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.79	0.82	96	empty
2	88	0.78	0.98	19	empty
3	705	0.76	0.81	69	empty
4	589	0.75	0.82	55	empty
5	159	0.44	0.75	22	empty

Interfaces

3 interfaces between chains.

A–B · 1204 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 1175 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 1165 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3DLI · Crystal structure of a SAM dependent methyltransferase from Archaeoglobus fulgidus · 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 O30190
Elsewhere: RCSB PDB 3DLI · PDBe 3DLI · UniProt O30190

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