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The complex of poph with peg

Analyse The complex of poph with peg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WWE
Type: protein
Length: 335 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidized polyvinyl alcohol hydrolase
EC: 3.7.1.7
UniProt: Q9LCQ7
Ligands: AE3
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxidized polyvinyl alcohol hydrolase (EC 3.7.1.7)	protein	335	27% helix, 24% strand	Q9LCQ7

Ligands and binding sites

AE3 · 2-(2-ethoxyethoxy)ethanol · ligand · 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	154	0.59	0.83	32	AE3
2	55	0.31	0.76	12	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

3WWE · The complex of pOPH with PEG · the same entry in another collection · chain A against A, TM-score 1.00
Q9LCQ7 · AlphaFold monomer V2.0 prediction for oxidized polyvinyl alcohol hydrolase (Q9LCQ7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9LCQ7
Elsewhere: RCSB PDB 3WWE · PDBe 3WWE · UniProt Q9LCQ7

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