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The glucuronoyl esterase OTCE15A H408A variant from opitutus terrae in complex with, and covalently linked to, D-glucuronate

Analyse The glucuronoyl esterase OTCE15A H408A variant from opitutus terrae in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SZ4
Type: protein
Length: 398 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: B1ZMF4
Ligands: BDP

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	398	—	B1ZMF4

Ligands and binding sites

BDP · beta-D-glucopyranuronic acid · sugar · chains A
FMT · Formic acid · additive · chains A

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

Compared structures

6SZ4 · The glucuronoyl esterase OtCE15A H408A variant from Opitutus terrae in complex with, and… · 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 6SZ4 · PDBe 6SZ4 · UniProt B1ZMF4

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