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Crystal structure of a C8-C4 SN3 inhibited esterase B from lactobacillus rhamnosis

Analyse Crystal structure of a C8-C4 SN3 inhibited esterase B from lactobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N5I
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ESTERASE/LIPASE
UniProt: C7TF14
Ligands: 2HD
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	ESTERASE/LIPASE	protein	311	46% helix, 18% strand	C7TF14

Ligands and binding sites

2HD · (2R)-2,3-dibutoxypropyl (R)-octylphosphinate · ligand · chains X
ACT · Acetate ion · additive · 2 copies · chains X

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	354	0.67	0.81	40	2HD
2	51	0.28	0.75	16	empty

Modifications

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

Compared structures

4N5I · Crystal Structure of a C8-C4 Sn3 Inhibited Esterase B from Lactobacillus Rhamnosis · the same entry in another collection · chain X against X, TM-score 1.00

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Every structure of UniProt C7TF14
Elsewhere: RCSB PDB 4N5I · PDBe 4N5I · UniProt C7TF14

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