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The wild type glucuronoyl esterase OTCE15A from opitutus terrae in complex with D-glucuronate

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: 6SYR
Type: protein
Length: 397 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucuronoyl esterase OTCE15A
UniProt: B1ZMF4
Ligands: GCU, MG, NA
Pockets: 3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucuronoyl esterase OTCE15A	protein	397	35% helix, 20% strand	B1ZMF4

Ligands and binding sites

GCU · alpha-D-glucopyranuronic acid · sugar · chains A
MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A

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

Pockets

3 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	155	0.44	0.75	23	empty
2	75	0.34	0.76	19	empty
3	75	0.34	0.76	18	GCU

Compared structures

6SYR · The wild type glucuronoyl esterase OtCE15A from Opitutus terrae in complex with… · 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 6SYR · PDBe 6SYR · UniProt B1ZMF4

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