MolNFT v1 · #134829 · protein

A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex

5TGL: “A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex”. X-ray diffraction, 1 ligand (HEE). MolNFT v1 #134829 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TGL
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P19515
Ligands: HEE

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	265	—	P19515

Ligands and binding sites

HEE · N-hexylphosphonate ethyl ester · ligand · chains A

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

Compared structures

5TGL · A model for interfacial activation in lipases from the structure of a fungal… · 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 0.97

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 5TGL · PDBe 5TGL · UniProt P19515

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