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Crystal structure of shaft pilin spaa from lactobacillus rhamnosus gg - E269A/D295N double mutant

Analyse Crystal structure of shaft pilin spaa from lactobacillus rhamnosus gg… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J4M
Type: protein
Length: 785 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell surface protein spaa
UniProt: C7T9P4
Pockets: 8 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cell surface protein spaa	protein	264	6% helix, 43% strand	C7T9P4
C	Cell surface protein spaa	protein	257	6% helix, 45% strand	C7T9P4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	257	0.54	0.76	33	empty
2	103	0.48	0.80	27	empty
3	157	0.43	0.74	27	empty
4	90	0.39	0.77	21	empty
5	90	0.34	0.75	20	empty

Interfaces

2 interfaces between chains.

A–B · 794 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 11 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 isopeptide (isopeptide).

Compared structures

5J4M · Crystal structure of shaft pilin SpaA from Lactobacillus rhamnosus GG - E269A/D295N… · the same entry in another collection · chain A against A, 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 C7T9P4
Elsewhere: RCSB PDB 5J4M · PDBe 5J4M · UniProt C7T9P4

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