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Crystal structure of the C-terminal domain of inva

Analyse Crystal structure of the C-terminal domain of inva in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X4A
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Invasion protein inva
UniProt: P0A1I3
Ligands: PO4
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Invasion protein inva	protein	327	50% helix, 20% strand	P0A1I3

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A
CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	306	0.68	0.83	44	CXS, PO4
2	87	0.54	0.85	24	empty
3	94	0.41	0.77	17	empty
4	59	0.34	0.77	17	empty

Compared structures

2X4A · Crystal structure of the C-terminal domain of InvA · the same entry in another collection · chain A against A, TM-score 1.00
P0A1I3 · AlphaFold monomer V2.0 prediction for invasion protein inva (P0A1I3) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0A1I3
Elsewhere: RCSB PDB 2X4A · PDBe 2X4A · UniProt P0A1I3

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