MolNFT v1 · #61536 · protein

Crystal structure of a thermostable esterase

3DOH: “Crystal structure of a thermostable esterase”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.60). MolNFT v1 #61536 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3DOH
Type: protein
Length: 748 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
UniProt: Q9WXP0
Ligands: SO4
Pockets: 5 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.1)	protein	375	24% helix, 34% strand	Q9WXP0
B	Esterase (EC 3.1.1.1)	protein	373	23% helix, 33% strand	Q9WXP0

Ligands and binding sites

SO4 · Sulfate ion · ion · 10 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	294	0.60	0.79	31	SO4
2	293	0.60	0.78	46	SO4
3	75	0.38	0.78	16	empty
4	133	0.37	0.73	23	empty
5	59	0.37	0.79	14	empty

Interfaces

1 interface between chains.

A–B · 586 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3DOH · Crystal Structure of a Thermostable 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 Q9WXP0
Elsewhere: RCSB PDB 3DOH · PDBe 3DOH · UniProt Q9WXP0

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