Research workbench

X-ray structure of Candida Antarctica lipase A

Analyse X-ray structure of Candida Antarctica lipase A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GUU
Type: protein
Length: 862 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Candida Antarctica
Molecule: Lipase A
EC: 3.1.1.3
Ligands: SO4
Pockets: 7 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase A (EC 3.1.1.3)	protein	431	42% helix, 18% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · chains B
1PE · Pentaethylene glycol · additive · 2 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

7 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	170	0.83	0.97	38	1PE
2	165	0.82	0.97	34	1PE
3	178	0.44	0.74	29	empty
4	127	0.44	0.77	20	empty
5	62	0.42	0.81	21	empty

Interfaces

1 interface between chains.

A–B · 568 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3GUU · X-ray structure of candida antarctica lipase a · 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 3GUU · PDBe 3GUU

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