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Crystal structure of apag protein from vibrio cholerae

Analyse Crystal structure of apag protein from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XVS
Type: protein
Length: 248 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein apag
UniProt: Q9KUS3
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 64% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein apag	protein	124	5% helix, 64% strand	Q9KUS3

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

2 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	207	0.67	0.85	20	empty
2	61	0.33	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 863 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1XVS · Crystal structure of apaG Protein from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
Q9KUS3 · AlphaFold monomer V2.0 prediction for protein apag (Q9KUS3) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9KUS3
Elsewhere: RCSB PDB 1XVS · PDBe 1XVS · UniProt Q9KUS3

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