MolNFT v1 · #130294 · protein

Humanized rat catechol O-methyltransferase in complex with 5-(4- fluorophenyl)-2,3-dihydroxy-N-(4-THIENO[2,3-C]PYRIDIN-2-ylbutyl) benzamide at 1.61A

5P92: “Humanized rat catechol O-methyltransferase in complex with 5-(4…”. X-ray diffraction, 5 ligands (76G, D1D, MG). MolNFT v1 #130294 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5P92
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P22734
Ligands: 76G, D1D, MG, CL, SO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	213	—	P22734

Ligands and binding sites

76G · 5-(4-fluorophenyl)-2,3-dihydroxy-N-(4-thieno[2,3-c]pyridin-2-ylbutyl)benzamide · ligand · chains A
D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A
NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A

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

Compared structures

5P92 · humanized rat catechol O-methyltransferase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · 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 P22734
Elsewhere: RCSB PDB 5P92 · PDBe 5P92 · UniProt P22734

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