Research workbench

Hia 992-1098

Analyse Hia 992-1098 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GR7
Type: protein
Length: 606 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adhesin
UniProt: Q48152
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Adhesin	protein	101	37% helix, 40% strand	Q48152

Ligands and binding sites

C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 5 copies · chains A, C, B, D, E

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

Pockets

5 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	801	0.70	0.76	79	C8E
2	78	0.38	0.77	18	empty
3	66	0.34	0.77	16	empty
4	59	0.33	0.77	14	empty
5	58	0.32	0.77	14	empty

Interfaces

9 interfaces between chains.

A–B · 1506 Å² buried · 23 hydrogen bonds · protein-protein
B–C · 1505 Å² buried · 23 hydrogen bonds · protein-protein
D–E · 1504 Å² buried · 24 hydrogen bonds · protein-protein
A–C · 1501 Å² buried · 24 hydrogen bonds · protein-protein
D–F · 1500 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

2GR7 · Hia 992-1098 · 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 Q48152
Elsewhere: RCSB PDB 2GR7 · PDBe 2GR7 · UniProt Q48152

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