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Catalytic domain of muty from escherichia COLI, D138N mutant complexed to adenine

Analyse Catalytic domain of muty from escherichia COLI, D138N mutant complexed to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MUD
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenine DNA glycosylase
EC: 3.2.2.31
UniProt: P17802
Ligands: ADE, SF4
Pockets: 1 · best druggability 0.50

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenine DNA glycosylase (EC 3.2.2.31)	protein	225	62% helix, 0% strand	P17802

Ligands and binding sites

ADE · Adenine · ligand · 2 copies · chains A
SF4 · Iron/sulfur cluster · ligand · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	151	0.50	0.79	28	ADE

Compared structures

1MUD · Catalytic domain of muty from escherichia COLI, D138N mutant complexed to adenine · 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 1MUD · PDBe 1MUD · UniProt P17802

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