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Self-complemented variant of fima, the main subunit of type 1 pilus

Analyse Self-complemented variant of fima, the main subunit of type 1 pilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JTY
Type: protein
Length: 184 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type-1 fimbrial protein, a chain
UniProt: P04128
Pockets: 1 · best druggability 0.28

Structure

solution nmr · 1 distinct chain · 5% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Type-1 fimbrial protein, a chain	protein	184	5% helix, 46% strand	P04128

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	67	0.28	0.73	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2JTY · Self-complemented variant of FimA, the main subunit of type 1 pilus · the same entry in another collection · chain A against A, TM-score 1.00
P04128 · AlphaFold monomer V2.0 prediction for type-1 fimbrial protein, a chain (P04128) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P04128
Elsewhere: RCSB PDB 2JTY · PDBe 2JTY · UniProt P04128

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