MolNFT v1 · #185420 · protein

CARM1 in complex with EML982

7PUQ: “CARM1 in complex with EML982”. X-ray diffraction, 1 ligand (867). MolNFT v1 #185420 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7PUQ
Type: protein
Length: 1,371 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9WVG6
Ligands: 867

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	—	protein	343	—	Q9WVG6
B	—	protein	343	—	Q9WVG6
D	—	protein	342	—	Q9WVG6

Ligands and binding sites

867 · methyl 6-[4-[[~{N}-[3-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]propyl]carbamimidoyl]amino]butylcarbamoylamino]-4-oxidanyl-naphthalene-2-carboxylate · ligand · 4 copies · chains A, B, C, D
EDO · 1,2-ethanediol · additive · 7 copies · chains A, B, C, D

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

Compared structures

7PUQ · CARM1 in complex with EML982 · the same entry in another collection · chain D against D, TM-score 1.00
Q9WVG6 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q9WVG6) · a predicted model of the same protein · 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 Q9WVG6
Elsewhere: RCSB PDB 7PUQ · PDBe 7PUQ · UniProt Q9WVG6

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