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NMR solution structure of zinc-binding protein 3-methyladenine DNA glycosylase I (tag)

Analyse NMR solution structure of zinc-binding protein 3-methyladenine DNA glycosylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NKU
Type: protein
Length: 187 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-methyladenine DNA glycosylase I (tag)
EC: 3.2.2.20
UniProt: P05100
Ligands: ZN
Pockets: 3 · best druggability 0.46

Structure

solution nmr · 1 distinct chain · 57% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-methyladenine DNA glycosylase I (tag) (EC 3.2.2.20)	protein	187	57% helix, 2% strand	P05100

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.46	0.78	21	empty
2	98	0.34	0.72	14	empty
3	50	0.33	0.78	15	empty

Compared structures

1NKU · NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG) · the same entry in another collection · chain A against A, TM-score 1.00
P05100 · AlphaFold monomer V2.0 prediction for DNA-3-methyladenine glycosylase 1 (P05100) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P05100
Elsewhere: RCSB PDB 1NKU · PDBe 1NKU · UniProt P05100

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