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Crystal structure of methyladenine demethylase

Analyse Crystal structure of methyladenine demethylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IE3
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleic acid dioxygenase ALKBH1
EC: 1.14.11.51
UniProt: Q13686
Ligands: MN
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.51)	protein	312	28% helix, 23% strand	Q13686

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A
EOH · Ethanol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	327	0.68	0.82	34	MN, EOH
2	101	0.42	0.78	16	empty
3	126	0.38	0.73	23	empty

Compared structures

6IE3 · Crystal structure of methyladenine demethylase · the same entry in another collection · chain A against A, TM-score 1.00
Q13686 · AlphaFold monomer V2.0 prediction for nucleic acid dioxygenase ALKBH1 (Q13686) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q13686
Elsewhere: RCSB PDB 6IE3 · PDBe 6IE3 · UniProt Q13686

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