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PH-induced modulation of streptococcus parasanguinis adhesion by FAP1 fimbriae

Analyse PH-induced modulation of streptococcus parasanguinis adhesion by FAP1 fimbriae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X12
Type: protein
Length: 400 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimbriae-associated protein FAP1
UniProt: Q9ZFF9
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fimbriae-associated protein FAP1	protein	200	6% helix, 48% strand	Q9ZFF9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.64	0.78	49	empty

Interfaces

1 interface between chains.

A–B · 891 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

2X12 · pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae · 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 Q9ZFF9
Elsewhere: RCSB PDB 2X12 · PDBe 2X12 · UniProt Q9ZFF9

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