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Structure of the corynebacterium diphtheriae major pilin spaa points to a modular pilus assembly stabilizing isopeptide bonds

Analyse Structure of the corynebacterium diphtheriae major pilin spaa points to a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HR6
Type: protein
Length: 420 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative surface-anchored fimbrial subunit
UniProt: Q6NF81
Ligands: CA, IOD
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative surface-anchored fimbrial subunit	protein	420	6% helix, 46% strand	Q6NF81

Ligands and binding sites

CA · Calcium ion · metal · chains A
IOD · Iodide ion · ion · chains A

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

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	76	0.34	0.75	17	empty
2	58	0.30	0.75	13	empty

Modifications

Observed in the structure: 2 isopeptide (isopeptide).

Compared structures

3HR6 · Structure of the Corynebacterium diphtheriae major pilin SpaA points to a modular pilus… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q6NF81
Elsewhere: RCSB PDB 3HR6 · PDBe 3HR6 · UniProt Q6NF81

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