MolNFT v1 · #161806 · protein

Rhizomucor miehei lipase propeptide complex, native

6QPP: “Rhizomucor miehei lipase propeptide complex, native”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.37). MolNFT v1 #161806 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6QPP
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: P19515
Ligands: NAG
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipase (EC 3.1.1.3)	protein	311	32% helix, 25% strand	P19515

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.37	0.76	21	empty

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6QPP · Rhizomucor miehei lipase propeptide complex, native · the same entry in another collection · chain A against A, TM-score 1.00
P19515 · AlphaFold monomer V2.0 prediction for lipase (P19515) · a predicted model of the same protein · 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 P19515
Elsewhere: RCSB PDB 6QPP · PDBe 6QPP · UniProt P19515

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