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Crystal structure of the yersinia enterocolitica type III secretion translocator chaperone sycd (alternative dimer)

Analyse Crystal structure of the yersinia enterocolitica type III secretion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VGY
Type: protein
Length: 132 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone sycd
UniProt: O87496
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone sycd	protein	132	78% helix, 0% strand	O87496

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.33	0.75	16	empty

Modifications

Observed in the structure: 9 modified (methylation).

Compared structures

2VGY · Crystal structure of the Yersinia enterocolitica Type III Secretion Translocator… · 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 O87496
Elsewhere: RCSB PDB 2VGY · PDBe 2VGY · UniProt O87496

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