MolNFT v1 · #128988 · protein

Structure of the inactive T.MARITIMA pde (TM1595) D80N D154N mutant with reaction products 2 AMP

5O70 · Phosphodiesterase: “Structure of the inactive T.MARITIMA pde (TM1595) D80N D154N mutant with reaction products 2 AMP”. X-ray diffraction, 2 ligands (AMP, SO4), 1 pocket (best druggability 0.79). MolNFT v1 #128988 on GenesisL1: 3D…

PDB: 5O70
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphodiesterase
UniProt: Q9X1T1
Ligands: AMP, SO4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphodiesterase	protein	323	44% helix, 19% strand	Q9X1T1

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 10 copies · chains A
GOL · Glycerol · additive · 2 copies · 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	1194	0.79	0.81	78	AMP, SO4, GOL

Compared structures

5O70 · Structure of the inactive T.maritima PDE (TM1595) D80N D154N mutant with reaction… · 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 Q9X1T1
Elsewhere: RCSB PDB 5O70 · PDBe 5O70 · UniProt Q9X1T1

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