MolNFT v1 · #61886 · protein

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

3DYV: “Snapshots of esterase D from lactobacillus rhamnosus: insights into a rotation driven catalytic mechanism”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.69). MolNFT v1 #61886 on GenesisL1: 3D structure, binding…

PDB: 3DYV
Type: protein
Length: 238 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase D
UniProt: B2CZF3
Ligands: CL
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase D	protein	238	47% helix, 16% strand	B2CZF3

Ligands and binding sites

CL · Chloride ion · ion · 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	259	0.69	0.84	42	CL

Compared structures

3DYV · 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 3DYV · PDBe 3DYV · UniProt B2CZF3

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