MolNFT v1 · #176425 · protein

Crystal structure of trans-methyltransferase calh complex with sah

7DMB · Putative methyltransferase: “Crystal structure of trans-methyltransferase calh complex with sah”. X-ray diffraction, 1 ligand (SAH), 6 pockets (best druggability 0.76). MolNFT v1 #176425 on GenesisL1: 3D structure, binding sites and…

PDB: 7DMB
Type: protein
Length: 716 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative methyltransferase
UniProt: A0A679DLY7
Ligands: SAH
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative methyltransferase	protein	358	48% helix, 18% strand	A0A679DLY7

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

6 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	502	0.76	0.83	52	SAH
2	430	0.73	0.83	49	SAH
3	359	0.70	0.83	39	empty
4	73	0.42	0.80	16	empty
5	51	0.33	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 470 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7DMB · Crystal structure of trans-methyltransferase CalH complex with SAH · 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 A0A679DLY7
Elsewhere: RCSB PDB 7DMB · PDBe 7DMB · UniProt A0A679DLY7

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