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Re-refined 1VCW, crystal structure of degs after backsoaking the activating peptide

Analyse Re-refined 1VCW, crystal structure of degs after backsoaking the activating… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RR0
Type: protein
Length: 818 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease degs
UniProt: H9UXC8
Pockets: 8 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease degs	protein	279	16% helix, 35% strand	H9UXC8
B	Protease degs	protein	268	18% helix, 35% strand	H9UXC8
C	Protease degs	protein	271	18% helix, 35% strand	H9UXC8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.66	0.97	17	empty
2	85	0.64	0.90	23	empty
3	164	0.60	0.83	24	empty
4	183	0.57	0.80	25	empty
5	219	0.49	0.75	46	empty

Interfaces

3 interfaces between chains.

A–C · 1015 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 953 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 953 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4RR0 · re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE · 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 H9UXC8
Elsewhere: RCSB PDB 4RR0 · PDBe 4RR0 · UniProt H9UXC8

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