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TPR3 of fimv from P. aeruginosa (PAO1)

Analyse TPR3 of fimv from P. aeruginosa (PAO1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MAL
Type: protein
Length: 123 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Motility protein fimv
UniProt: Q9HZA6

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Motility protein fimv	protein	59	75% helix, 0% strand	Q9HZA6
B	Motility protein fimv	protein	64	72% helix, 0% strand	Q9HZA6

Interfaces

1 interface between chains.

A–B · 432 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4MAL · TPR3 of FimV from P. aeruginosa (PAO1) · the same entry in another collection · chain A against A, TM-score 1.00
Q9HZA6 · AlphaFold monomer V2.0 prediction for motility hub protein fimv (Q9HZA6) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 Q9HZA6
Elsewhere: RCSB PDB 4MAL · PDBe 4MAL · UniProt Q9HZA6

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