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Crystal structure of T1 lipase F16L mutant

Analyse Crystal structure of T1 lipase F16L mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z5G
Type: protein
Length: 774 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermostable lipase
EC: 3.1.1.3
UniProt: Q842J9
Ligands: ZN, CA, CL
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thermostable lipase (EC 3.1.1.3)	protein	387	39% helix, 16% strand	Q842J9

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

4 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	776	0.71	0.77	69	empty
2	195	0.54	0.79	23	empty
3	102	0.34	0.73	17	empty
4	84	0.32	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 434 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2Z5G · Crystal structure of T1 lipase F16L mutant · 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 Q842J9
Elsewhere: RCSB PDB 2Z5G · PDBe 2Z5G · UniProt Q842J9

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