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Crystal structure of the HMW1 secretion domain from haemophilus influenzae

Analyse Crystal structure of the HMW1 secretion domain from haemophilus influenzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ODL
Type: protein
Length: 372 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adhesin
UniProt: Q48031
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adhesin	protein	372	4% helix, 53% strand	Q48031

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.43	0.74	26	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2ODL · Crystal structure of the HMW1 secretion domain from Haemophilus influenzae · 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 Q48031
Elsewhere: RCSB PDB 2ODL · PDBe 2ODL · UniProt Q48031

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