MolNFT v1 · #107678 · protein

Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound)

4UHE: “Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound)”. X-ray diffraction, 2 ligands (MLT, CL), 2 pockets (best druggability 0.58). MolNFT v1 #107678 on GenesisL1: 3D structure, binding sites and…

PDB: 4UHE
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
Ligands: MLT, CL
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.1)	protein	272	49% helix, 18% strand	—

Ligands and binding sites

MLT · D-malate · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A
PGE · Triethylene 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.58	0.79	29	CL, MLT
2	61	0.30	0.75	16	empty

Compared structures

4UHE · Structural studies of a thermophilic esterase from Thermogutta terrifontis (malate bound) · 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
Elsewhere: RCSB PDB 4UHE · PDBe 4UHE

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