MolNFT v2 · #170388 · protein

Crystal structure of human phenylethanolamine N-methyltransferase (PNMT) in complex with (2S)-2-amino-4-((((2R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(3-(7,8-dichloro-1,2,3,4-tetrahydroisoquinolin-4-yl)propyl)amino)butanoic acid and AdoHcy (SAH)

6WS1: “Crystal structure of human phenylethanolamine N-methyltransferase (PNMT) in complex with…”. X-ray diffraction at 2.76, 2 ligands (CD, K). MolNFT v2 #170388 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6WS1
Type: protein
Length: 528 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.76
Source: Homo sapiens
UniProt: P11086
Ligands: CD, K

Structure

x-ray diffraction · resolution 2.76 · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	261	—	P11086
B	—	protein	267	—	P11086

Ligands and binding sites

CD · Cadmium ion · metal · chains A
K · Potassium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Compared structures

6WS1 · Crystal structure of human phenylethanolamine N-methyltransferase (pnmt) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P11086 · AlphaFold monomer V2.0 prediction for phenylethanolamine N-methyltransferase (P11086) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P11086
Elsewhere: RCSB PDB 6WS1 · PDBe 6WS1 · UniProt P11086

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