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Crystal structure of PRMT6-sah

Analyse Crystal structure of PRMT6-sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LWP
Type: protein
Length: 683 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginine N-methyltransferase, putative
UniProt: Q57U70
Ligands: SAH, IOD
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Arginine N-methyltransferase, putative	protein	342	36% helix, 29% strand	Q57U70
A	Arginine N-methyltransferase, putative	protein	341	36% helix, 29% strand	Q57U70

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains B, A
IOD · Iodide ion · ion · 9 copies · chains B, A
PGE · Triethylene glycol · additive · chains A

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	242	0.60	0.80	36	SAH
2	285	0.57	0.77	38	IOD, SAH
3	128	0.39	0.74	20	PGE
4	75	0.33	0.75	12	empty

Interfaces

1 interface between chains.

B–A · 1633 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4LWP · Crystal structure of PRMT6-SAH · 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 Q57U70
Elsewhere: RCSB PDB 4LWP · PDBe 4LWP · UniProt Q57U70

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