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The structure of haemophilus influenzae protein E

Analyse The structure of haemophilus influenzae protein E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZH5
Type: protein
Length: 264 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein E
UniProt: C4F5U7
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein E	protein	132	11% helix, 48% strand	C4F5U7
B	Protein E	protein	132	9% helix, 48% strand	C4F5U7

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

2 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	172	0.67	0.87	25	EDO
2	535	0.65	0.77	49	empty

Interfaces

1 interface between chains.

A–B · 698 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3ZH5 · The structure of Haemophilus influenzae protein E · 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 C4F5U7
Elsewhere: RCSB PDB 3ZH5 · PDBe 3ZH5 · UniProt C4F5U7

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