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Crystal structure of brevundimonas diminuta phosphotriesterase mutant L7EP-3AG

Analyse Crystal structure of brevundimonas diminuta phosphotriesterase mutant L7EP-3AG in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZSU
Type: protein
Length: 658 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: CO
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Parathion hydrolase (EC 3.1.8.1)	protein	329	50% helix, 14% strand	P0A434

Ligands and binding sites

CO · Cobalt (II) ion · metal · 4 copies · chains A, B

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

Pockets

4 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	99	0.66	0.91	27	empty
2	189	0.61	0.83	34	CO
3	193	0.60	0.82	33	empty
4	59	0.32	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1386 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (carboxylation).

Compared structures

4ZSU · Crystal structure of Brevundimonas diminuta phosphotriesterase mutant L7eP-3aG · the same entry in another collection · chain A against A, TM-score 1.00

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 4ZSU · PDBe 4ZSU · UniProt P0A434

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