Research workbench

M. smegmatis antimutator protein MUTT2 in complex with dctp

Analyse M. smegmatis antimutator protein MUTT2 in complex with dctp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZRK
Type: protein
Length: 256 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative mutator protein MUTT2/NUDIX hydrolase
UniProt: I7FJF7
Ligands: DCP
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative mutator protein MUTT2/NUDIX hydrolase	protein	129	24% helix, 40% strand	I7FJF7
B	Putative mutator protein MUTT2/NUDIX hydrolase	protein	127	23% helix, 43% strand	I7FJF7

Ligands and binding sites

DCP · 2'-deoxycytidine-5'-triphosphate · ligand · 2 copies · chains A, B

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	155	0.50	0.78	26	DCP
2	149	0.47	0.77	24	DCP

Interfaces

1 interface between chains.

A–B · 199 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5ZRK · M. smegmatis antimutator protein MutT2 in complex with dCTP · the same entry in another collection · chain A against A, TM-score 1.00

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 I7FJF7
Elsewhere: RCSB PDB 5ZRK · PDBe 5ZRK · UniProt I7FJF7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.