MolNFT v1 · #16741 · protein

Tryparedoxin II from C.FASCICULATA solved by sulphur phasing

1O81: “Tryparedoxin II from C.FASCICULATA solved by sulphur phasing”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.37). MolNFT v1 #16741 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1O81
Type: protein
Length: 296 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryparedoxin II
UniProt: O77093
Ligands: SO4
Pockets: 4 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryparedoxin II	protein	152	35% helix, 21% strand	O77093
B	Tryparedoxin II	protein	144	32% helix, 24% strand	O77093

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

4 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	82	0.37	0.76	19	empty
2	73	0.32	0.74	14	empty
3	66	0.32	0.75	18	SO4
4	74	0.27	0.72	17	empty

Interfaces

1 interface between chains.

A–B · 664 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1O81 · Tryparedoxin II from C.fasciculata solved by sulphur phasing · 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 O77093
Elsewhere: RCSB PDB 1O81 · PDBe 1O81 · UniProt O77093

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