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Hia 1022-1098

Analyse Hia 1022-1098 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GR8
Type: protein
Length: 468 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Haemophilus influenzae
Molecule: Adhesin
UniProt: Q48152
Pockets: 4 · best druggability 0.49

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 17% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Adhesin	protein	78	17% helix, 51% strand	Q48152

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.49	0.81	19	empty
2	211	0.47	0.74	32	empty
3	56	0.28	0.74	16	empty
4	50	0.27	0.74	14	empty

Interfaces

10 interfaces between chains.

B–E · 1146 Å² buried · 26 hydrogen bonds · protein-protein
A–D · 1116 Å² buried · 23 hydrogen bonds · protein-protein
C–D · 1115 Å² buried · 22 hydrogen bonds · protein-protein
A–C · 1110 Å² buried · 21 hydrogen bonds · protein-protein
E–F · 1094 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

2GR8 · Hia 1022-1098 · 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 2GR8 · PDBe 2GR8 · UniProt Q48152

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