MolNFT v1 · #164466 · protein

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

6SYU: “The wild type glucuronoyl esterase OTCE15A from opitutus terrae in complex with xylobiose”. X-ray diffraction, 2 ligands (XYP, MG), 2 pockets (best druggability 0.40). MolNFT v1 #164466 on GenesisL1: 3D structure, binding sites and…

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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