MolNFT v1 · #61963 · protein

Snapshots of esterase D from lactobacillus rhamnosus: insights into a rotation driven catalytic mechanism

3E1G: “Snapshots of esterase D from lactobacillus rhamnosus: insights into a rotation driven catalytic mechanism”. X-ray diffraction, 1 ligand (DEP), 1 pocket (best druggability 0.67). MolNFT v1 #61963 on GenesisL1: 3D structure, binding…

PDB: 3E1G
Type: protein
Length: 239 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase D
UniProt: B2CZF3
Ligands: DEP
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase D	protein	239	48% helix, 15% strand	B2CZF3

Ligands and binding sites

DEP · Diethyl phosphonate · ligand · 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	234	0.67	0.84	40	DEP

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3E1G · Snapshots of esterase D from lactobacillus rhamnosus: Insights into a rotation driven… · 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 B2CZF3
Elsewhere: RCSB PDB 3E1G · PDBe 3E1G · UniProt B2CZF3

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