MolNFT v1 · #107676 · protein

Structural studies of a thermophilic esterase from thermogutta terrifontis (native)

4UHC: “Structural studies of a thermophilic esterase from thermogutta terrifontis (native)”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.57). MolNFT v1 #107676 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4UHC
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
Ligands: CL
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.1)	protein	278	50% helix, 18% strand	—

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	219	0.57	0.79	23	CL

Compared structures

4UHC · Structural studies of a thermophilic esterase from Thermogutta terrifontis (Native) · 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 4UHC · PDBe 4UHC

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