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Crystal structure of thermostable, organic-solvent tolerant lipase from geobacillus sp. strain arm

Analyse Crystal structure of thermostable, organic-solvent tolerant lipase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FMP
Type: protein
Length: 762 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: Q93A71
Ligands: ZN, CA
Pockets: 6 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase (EC 3.1.1.3)	protein	381	40% helix, 16% strand	Q93A71

Ligands and binding sites

ZN · Zinc ion · metal · 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

6 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	190	0.56	0.79	22	empty
2	198	0.55	0.79	25	empty
3	57	0.47	0.85	16	empty
4	232	0.45	0.73	37	empty
5	66	0.40	0.80	24	empty

Interfaces

1 interface between chains.

A–B · 675 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4FMP · Crystal structure of thermostable, organic-solvent tolerant lipase from Geobacillus sp.… · 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 Q93A71
Elsewhere: RCSB PDB 4FMP · PDBe 4FMP · UniProt Q93A71

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