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Structure of the citrobacter freundii effector binding domain containing three amino acid substitutions: T103V, S221A and Y264F

Analyse Structure of the citrobacter freundii effector binding domain containing three… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KOT
Type: protein
Length: 198 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hth-type transcriptional activator ampr
UniProt: P12529
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hth-type transcriptional activator ampr	protein	198	36% helix, 29% strand	P12529

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · 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	145	0.63	0.86	25	GOL
2	50	0.30	0.76	14	empty

Compared structures

3KOT · Structure of the Citrobacter freundii effector binding domain containing three amino acid… · the same entry in another collection · chain A against A, TM-score 1.00
P12529 · AlphaFold monomer V2.0 prediction for hth-type transcriptional activator ampr (P12529) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P12529
Elsewhere: RCSB PDB 3KOT · PDBe 3KOT · UniProt P12529

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