Research workbench

Pilus-presented adhesin, SPY0125 (cpa), P1 form

Analyse Pilus-presented adhesin, SPY0125 (cpa), P1 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XI9
Type: protein
Length: 614 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ancillary protein 1
UniProt: Q8GRA2
Pockets: 8 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ancillary protein 1	protein	304	20% helix, 31% strand	Q8GRA2
B	Ancillary protein 1	protein	310	20% helix, 30% strand	Q8GRA2

Pockets

8 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	905	0.79	0.81	76	empty
2	220	0.49	0.74	28	empty
3	193	0.48	0.75	21	empty
4	98	0.46	0.80	20	empty
5	90	0.46	0.80	17	empty

Interfaces

1 interface between chains.

A–B · 664 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified, 2 isopeptide (engineered, isopeptide).

Compared structures

2XI9 · Pilus-presented adhesin, Spy0125 (Cpa), P1 form · 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 Q8GRA2
Elsewhere: RCSB PDB 2XI9 · PDBe 2XI9 · UniProt Q8GRA2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.