MolNFT v1 · #81642 · protein

Structure of the fimbrial protein fimp from actonomyces oris

3UXF · Fimbrial subunit type 1: “Structure of the fimbrial protein fimp from actonomyces oris”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.45). MolNFT v1 #81642 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3UXF
Type: protein
Length: 449 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimbrial subunit type 1
UniProt: P18477
Ligands: CA
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fimbrial subunit type 1	protein	449	8% helix, 40% strand	P18477

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	194	0.45	0.74	28	empty
2	58	0.39	0.81	12	empty
3	120	0.38	0.73	25	empty
4	66	0.32	0.75	16	empty

Modifications

Observed in the structure: 2 disulfide, 2 isopeptide (disulfide, isopeptide).

Compared structures

3UXF · Structure of the fimbrial protein FimP from Actonomyces oris · the same entry in another collection · chain A against A, TM-score 1.00
P18477 · AlphaFold monomer V2.0 prediction for fimbrial subunit type 1 (P18477) · a predicted model of the same protein · chain A against A, TM-score 0.74

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 P18477
Elsewhere: RCSB PDB 3UXF · PDBe 3UXF · UniProt P18477

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