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Phosphotriesterase PTE_A53_1

Analyse Phosphotriesterase PTE_A53_1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FEI
Type: protein
Length: 664 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Parathion hydrolase
EC: 3.1.8.1
UniProt: P0A434
Ligands: D6K, ZN
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Parathion hydrolase (EC 3.1.8.1)	protein	327	52% helix, 14% strand	P0A434
B	Parathion hydrolase (EC 3.1.8.1)	protein	337	51% helix, 14% strand	P0A434

Ligands and binding sites

D6K · (4~{S},6~{R})-2,2,6-trimethyl-1,3-dioxan-4-ol · ligand · chains A
ZN · Zinc ion · metal · 4 copies · chains A, B
FMT · Formic acid · additive · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.66	0.82	35	ZN, D6K
2	296	0.65	0.81	36	FMT, ZN
3	152	0.64	0.86	30	empty
4	67	0.34	0.76	14	empty
5	60	0.32	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1449 Å² buried · 37 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (additive adduct).

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 P0A434
Elsewhere: RCSB PDB 6FEI · PDBe 6FEI · UniProt P0A434

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