MolNFT v1 · #26079 · protein

Catalytic domain of muty from escherichia COLI K142A mutant

1WEG · A/G-specific adenine glycosylase: “Catalytic domain of muty from escherichia COLI K142A mutant”. X-ray diffraction, 1 ligand (SF4), 2 pockets (best druggability 0.57). MolNFT v1 #26079 on GenesisL1: 3D structure, binding sites and…

PDB: 1WEG
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: A/G-specific adenine glycosylase
EC: 3.2.2.-
UniProt: P17802
Ligands: SF4
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	A/G-specific adenine glycosylase (EC 3.2.2.-)	protein	225	62% helix, 0% strand	P17802

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
IMD · Imidazole · additive · 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	267	0.57	0.77	40	IMD
2	51	0.24	0.72	15	empty

Compared structures

1WEG · Catalytic Domain Of Muty From Escherichia Coli K142A Mutant · the same entry in another collection · chain A against A, TM-score 1.00
P17802 · AlphaFold monomer V2.0 prediction for adenine DNA glycosylase (P17802) · 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 P17802
Elsewhere: RCSB PDB 1WEG · PDBe 1WEG · UniProt P17802

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