Research workbench

Triple mutant gravn

Analyse Triple mutant gravn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J4Y
Type: protein
Length: 997 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Np protein
UniProt: E2DQZ4
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 65% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Np protein	protein	250	63% helix, 1% strand	E2DQZ4
B, D	Np protein	protein	248	65% helix, 1% strand	E2DQZ4
C	Np protein	protein	251	66% helix, 1% strand	E2DQZ4

Pockets

6 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	1154	0.79	0.81	98	empty
2	1194	0.78	0.80	102	empty
3	146	0.47	0.77	25	empty
4	107	0.40	0.76	20	empty
5	86	0.40	0.77	21	empty

Interfaces

5 interfaces between chains.

A–D · 1751 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1711 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1546 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1540 Å² buried · 16 hydrogen bonds · protein-protein
B–D · 98 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4J4Y · Triple mutant GraVN · 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 E2DQZ4
Elsewhere: RCSB PDB 4J4Y · PDBe 4J4Y · UniProt E2DQZ4

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