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Structure of PROTEASE1 from pyrococcus horikoshii at room temperature in chipx microfluidic device

Analyse Structure of PROTEASE1 from pyrococcus horikoshii at room temperature in chipx… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q3T
Type: protein
Length: 498 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deglycase PH1704
EC: 3.5.1.124, 3.4.22.-
UniProt: O59413
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Deglycase PH1704 (EC 3.5.1.124, 3.4.22.-)	protein	166	39% helix, 25% strand	O59413

Pockets

3 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	179	0.56	0.81	29	empty
2	103	0.38	0.75	15	empty
3	80	0.37	0.76	15	empty

Interfaces

2 interfaces between chains.

A–B · 874 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 767 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6Q3T · Structure of Protease1 from Pyrococcus horikoshii at room temperature in ChipX… · the same entry in another collection · chain A against A, TM-score 1.00
O59413 · AlphaFold monomer V2.0 prediction for deglycase PH1704 (O59413) · a predicted model of the same protein · chain B 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 O59413
Elsewhere: RCSB PDB 6Q3T · PDBe 6Q3T · UniProt O59413

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