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

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PDB: 3HTL
Type: protein
Length: 422 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, NA
Pockets: 3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Putative surface-anchored fimbrial subunit	protein	422	6% helix, 45% strand	Q6NF81

Ligands and binding sites

CA · Calcium ion · metal · chains X
NA · Sodium ion · metal · chains X

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

Pockets

3 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	74	0.35	0.76	18	empty
2	84	0.33	0.75	23	empty
3	61	0.29	0.74	17	empty

Modifications

Observed in the structure: 4 modified, 2 isopeptide (engineered, isopeptide).

Compared structures

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

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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 3HTL · PDBe 3HTL · UniProt Q6NF81

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