Research workbench

A. fulgidus lipase with fatty acid fragment and calcium

Analyse A. fulgidus lipase with fatty acid fragment and calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZYI
Type: protein
Length: 900 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase, putative
EC: 3.1.1.3
UniProt: O28511
Ligands: STE, CA
Pockets: 10 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase, putative (EC 3.1.1.3)	protein	450	28% helix, 29% strand	O28511

Ligands and binding sites

STE · Stearic acid · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	517	0.85	0.91	80	STE
2	650	0.83	0.87	95	STE
3	178	0.64	0.84	25	empty
4	180	0.63	0.84	24	empty
5	234	0.53	0.76	35	empty

Interfaces

1 interface between chains.

A–B · 524 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2ZYI · A. Fulgidus lipase with fatty acid fragment and calcium · 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 O28511
Elsewhere: RCSB PDB 2ZYI · PDBe 2ZYI · UniProt O28511

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