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MTH0212 with two bound manganese ions

Analyse MTH0212 with two bound manganese ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G0A
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exodeoxyribonuclease
EC: 3.1.11.2
UniProt: O26314
Ligands: MN, PO4
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exodeoxyribonuclease (EC 3.1.11.2)	protein	257	28% helix, 26% strand	O26314

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	207	0.48	0.75	32	MN
2	61	0.31	0.75	16	empty

Compared structures

3G0A · Mth0212 with two bound manganese ions · the same entry in another collection · chain A against A, TM-score 1.00
O26314 · AlphaFold monomer V2.0 prediction for DNA uridine endonuclease (O26314) · 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 O26314
Elsewhere: RCSB PDB 3G0A · PDBe 3G0A · UniProt O26314

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