Research workbench

Crystal structure of pul and PFU(MUTATE) domain

Analyse Crystal structure of pul and PFU(MUTATE) domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PST
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein DOA1
UniProt: P36037
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein DOA1	protein	317	65% helix, 5% strand	P36037

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	249	0.57	0.78	30	empty
2	275	0.54	0.76	31	empty
3	64	0.42	0.81	16	empty
4	58	0.28	0.74	14	empty

Compared structures

3PST · Crystal structure of PUL and PFU(mutate) domain · the same entry in another collection · chain A against A, TM-score 1.00
P36037 · AlphaFold monomer V2.0 prediction for protein DOA1 (P36037) · 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 P36037
Elsewhere: RCSB PDB 3PST · PDBe 3PST · UniProt P36037

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