MolNFT v1 · #5414 · protein

Methylated human O6-alkylguanine-DNA alkyltransferase

1EH7: “Methylated human O6-alkylguanine-DNA alkyltransferase”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.44). MolNFT v1 #5414 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EH7
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O6-alkylguanine-DNA alkyltransferase
EC: 2.1.1.63
UniProt: P16455
Ligands: ZN
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	O6-alkylguanine-DNA alkyltransferase (EC 2.1.1.63)	protein	162	40% helix, 16% strand	P16455

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.44	0.81	15	empty

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

1EH7 · Methylated human O6-alkylguanine-DNA alkyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
P16455 · AlphaFold monomer V2.0 prediction for methylated-DNA--protein- cysteine methyltransferase… · 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 P16455
Elsewhere: RCSB PDB 1EH7 · PDBe 1EH7 · UniProt P16455

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