Research workbench

Ustilago maydis lipase UM03410, short form without flap

Analyse Ustilago maydis lipase UM03410, short form without flap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZPX
Type: protein
Length: 764 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: Q4P903
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase (EC 3.1.1.3)	protein	382	44% helix, 18% strand	Q4P903

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · chains A
PG4 · Tetraethylene glycol · additive · chains B

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

Pockets

2 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	1136	0.86	0.86	112	empty
2	112	0.78	0.97	29	empty

Interfaces

1 interface between chains.

A–B · 1059 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3ZPX · Ustilago maydis lipase UM03410, short form without flap · 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 Q4P903
Elsewhere: RCSB PDB 3ZPX · PDBe 3ZPX · UniProt Q4P903

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.