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Crystal structure of HMTH1 D120N in the presence of acetate

Analyse Crystal structure of HMTH1 D120N in the presence of acetate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GLT
Type: protein
Length: 154 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 7,8-dihydro-8-oxoguanine triphosphatase
EC: 3.6.1.55, 3.6.1.56
UniProt: P36639
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	7,8-dihydro-8-oxoguanine triphosphatase (EC 3.6.1.55, 3.6.1.56)	protein	154	18% helix, 46% strand	P36639

Ligands and binding sites

DMS · Dimethyl sulfoxide · 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	224	0.65	0.83	30	DMS

Compared structures

6GLT · Crystal structure of hMTH1 D120N in the presence of acetate · the same entry in another collection · chain A against A, TM-score 1.00
P36639 · AlphaFold monomer V2.0 prediction for 7,8-dihydro-8-oxoguanine triphosphatase (P36639) · 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 P36639
Elsewhere: RCSB PDB 6GLT · PDBe 6GLT · UniProt P36639

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