Research workbench

Clostridium thermocellum family 3 carbohydrate esterase

Analyse Clostridium thermocellum family 3 carbohydrate esterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VPT
Type: protein
Length: 201 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipolytic enzyme
EC: 3.1.1.72
UniProt: A3DDK4
Ligands: CA
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipolytic enzyme (EC 3.1.1.72)	protein	201	48% helix, 17% strand	A3DDK4

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.48	0.84	15	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

2VPT · Clostridium thermocellum family 3 carbohydrate esterase · 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 A3DDK4
Elsewhere: RCSB PDB 2VPT · PDBe 2VPT · UniProt A3DDK4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.