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Orthorhombic crystal structure of salmonella flga in closed form

Analyse Orthorhombic crystal structure of salmonella flga in closed form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VJP
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagella basal body P-ring formation protein flga
UniProt: P40131
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Flagella basal body P-ring formation protein flga	protein	198	8% helix, 46% strand	P40131

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	163	0.43	0.74	29	empty
2	117	0.38	0.74	18	empty
3	100	0.34	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 661 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 2 disulfide (engineered, disulfide).

Compared structures

3VJP · Orthorhombic Crystal Structure of Salmonella FlgA in closed form · the same entry in another collection · chain A against A, TM-score 1.00
P40131 · AlphaFold monomer V2.0 prediction for flagella basal body P-ring formation protein flga… · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P40131
Elsewhere: RCSB PDB 3VJP · PDBe 3VJP · UniProt P40131

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