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The wild type glucuronoyl esterase OTCE15A from opitutus terrae in complex with xylobiose

Analyse The wild type glucuronoyl esterase OTCE15A from opitutus terrae in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SYU
Type: protein
Length: 402 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucuronoyl esterase OTCE15A
UniProt: B1ZMF4
Ligands: XYP, MG
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucuronoyl esterase OTCE15A	protein	402	34% helix, 21% strand	B1ZMF4

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 4 copies · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
PG4 · Tetraethylene glycol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.40	0.75	23	XYP
2	52	0.39	0.82	17	empty

Compared structures

6SYU · The wild type glucuronoyl esterase OtCE15A from Opitutus terrae in complex with xylobiose · 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 B1ZMF4
Elsewhere: RCSB PDB 6SYU · PDBe 6SYU · UniProt B1ZMF4

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