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Crystal structure of bcpa, the major pilin subunit of bacillus cereus

Analyse Crystal structure of bcpa, the major pilin subunit of bacillus cereus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KPT
Type: protein
Length: 705 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen adhesion protein
UniProt: Q81D71
Ligands: CA
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen adhesion protein	protein	350	3% helix, 55% strand	Q81D71
B	Collagen adhesion protein	protein	355	3% helix, 55% strand	Q81D71

Ligands and binding sites

CA · Calcium ion · metal · chains B

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	290	0.49	0.73	36	empty
2	106	0.48	0.80	22	empty

Interfaces

1 interface between chains.

A–B · 111 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 6 isopeptide (engineered, isopeptide).

Compared structures

3KPT · Crystal structure of BcpA, the major pilin subunit of Bacillus cereus · 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 Q81D71
Elsewhere: RCSB PDB 3KPT · PDBe 3KPT · UniProt Q81D71

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