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NMR structure of the E. COLI type 1 pilus subunit fimf

Analyse NMR structure of the E. COLI type 1 pilus subunit fimf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JMR
Type: protein
Length: 179 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimf
UniProt: P08189
Pockets: 2 · best druggability 0.45

Structure

solution nmr · 1 distinct chain · 6% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fimf	protein	179	6% helix, 27% strand	P08189

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.45	0.84	22	empty
2	74	0.30	0.73	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2JMR · NMR structure of the E. coli type 1 pilus subunit FimF · the same entry in another collection · chain A against A, TM-score 1.00
P08189 · AlphaFold monomer V2.0 prediction for protein fimf (P08189) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P08189
Elsewhere: RCSB PDB 2JMR · PDBe 2JMR · UniProt P08189

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