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Crystal structure of Haemophilus influenzae HiaBD2

Analyse Crystal structure of Haemophilus influenzae HiaBD2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EMF
Type: protein
Length: 336 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Haemophilus influenzae
Molecule: Hia (Adhesin)
UniProt: Q48152
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 14% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Hia (Adhesin)	protein	113	12% helix, 35% strand	Q48152
B	Hia (Adhesin)	protein	110	15% helix, 40% strand	Q48152

Pockets

4 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	118	0.79	0.98	22	empty
2	112	0.41	0.77	22	empty
3	87	0.38	0.77	22	empty
4	85	0.35	0.76	20	empty

Interfaces

3 interfaces between chains.

B–C · 1935 Å² buried · 44 hydrogen bonds · protein-protein
A–C · 1914 Å² buried · 47 hydrogen bonds · protein-protein
A–B · 1887 Å² buried · 44 hydrogen bonds · protein-protein

Compared structures

3EMF · Crystal structure of haemophilus influenzae HIABD2 · 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 3EMF · PDBe 3EMF · UniProt Q48152

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