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Deoxychorismate lyase from escherichia COLI with inhibitor

Analyse Deoxychorismate lyase from escherichia COLI with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1I2L
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-amino-4-deoxychorismate lyase
EC: 4.-.-.-
UniProt: P28305
Ligands: DCS
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-amino-4-deoxychorismate lyase (EC 4.-.-.-)	protein	269	28% helix, 30% strand	P28305

Ligands and binding sites

DCS · D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide · ligand · chains A

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

Pockets

3 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	266	0.60	0.79	34	DCS
2	55	0.32	0.77	11	empty
3	53	0.25	0.72	16	empty

Compared structures

1I2L · Deoxychorismate lyase from escherichia COLI with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
P28305 · AlphaFold monomer V2.0 prediction for aminodeoxychorismate lyase (P28305) · 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 P28305
Elsewhere: RCSB PDB 1I2L · PDBe 1I2L · UniProt P28305

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