MolNFT v1 · #30512 · protein

Crystal structure of human indolethylamine N- methyltransferase with sah

2A14 · Indolethylamine N-methyltransferase: “Crystal structure of human indolethylamine N- methyltransferase with sah”. X-ray diffraction, 2 ligands (SAH, SO4), 2 pockets (best druggability 0.76). MolNFT v1 #30512 on GenesisL1: 3D…

PDB: 2A14
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Indolethylamine N-methyltransferase
EC: 2.1.1.49
UniProt: O95050
Ligands: SAH, SO4
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Indolethylamine N-methyltransferase (EC 2.1.1.49)	protein	257	39% helix, 25% strand	O95050

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.76	0.93	31	SAH
2	100	0.43	0.78	18	empty

Compared structures

2A14 · Crystal Structure of Human Indolethylamine N-methyltransferase with SAH · the same entry in another collection · chain A against A, TM-score 1.00
O95050 · AlphaFold monomer V2.0 prediction for indolethylamine N-methyltransferase (O95050) · 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 O95050
Elsewhere: RCSB PDB 2A14 · PDBe 2A14 · UniProt O95050

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