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Supercharged arpte variant R5

Analyse Supercharged arpte variant R5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W7H
Type: protein
Length: 658 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotriesterase
UniProt: Q93LD7
Ligands: ZN
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotriesterase	protein	329	49% helix, 13% strand	Q93LD7
B	Phosphotriesterase	protein	329	51% helix, 13% strand	Q93LD7

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

7 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	139	0.72	0.92	29	empty
2	236	0.59	0.80	32	empty
3	190	0.58	0.81	34	empty
4	61	0.47	0.84	17	empty
5	88	0.43	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 1493 Å² buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (carboxylation).

Compared structures

5W7H · Supercharged arPTE variant R5 · 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 Q93LD7
Elsewhere: RCSB PDB 5W7H · PDBe 5W7H · UniProt Q93LD7

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