Research workbench

Pilus-presented adhesin, SPY0125 (cpa), P212121 form (esrf data)

Analyse Pilus-presented adhesin, SPY0125 (cpa), P212121 form (esrf data) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XIC
Type: protein
Length: 847 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ancillary protein 1
UniProt: Q8GRA2
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ancillary protein 1	protein	422	13% helix, 40% strand	Q8GRA2
B	Ancillary protein 1	protein	425	13% helix, 39% strand	Q8GRA2

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	784	0.81	0.84	103	empty
2	482	0.61	0.75	48	empty
3	79	0.51	0.84	18	empty
4	65	0.34	0.77	15	empty
5	56	0.32	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 974 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified, 4 isopeptide (engineered, isopeptide).

Compared structures

2XIC · Pilus-presented adhesin, Spy0125 (Cpa), P212121 form (ESRF data) · 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 2XIC · PDBe 2XIC · UniProt Q8GRA2

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