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Crystal structure of the truncated K122-4 pilin from pseudomonas aeruginosa

Analyse Crystal structure of the truncated K122-4 pilin from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QVE
Type: protein
Length: 251 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimbrial protein
UniProt: P17838
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fimbrial protein	protein	126	30% helix, 28% strand	P17838
B	Fimbrial protein	protein	125	30% helix, 28% strand	P17838

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	169	0.43	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 170 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1QVE · Crystal structure of the truncated K122-4 pilin from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
P17838 · AlphaFold monomer V2.0 prediction for fimbrial protein (P17838) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P17838
Elsewhere: RCSB PDB 1QVE · PDBe 1QVE · UniProt P17838

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