Research workbench

Crystal structure of human PIN1 complexed with covalent inhibitor

Analyse Crystal structure of human PIN1 complexed with covalent inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EFX
Type: protein
Length: 147 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase nima-interacting 1
EC: 5.2.1.8
UniProt: Q13526
Ligands: J3X
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	147	27% helix, 24% strand	Q13526

Ligands and binding sites

J3X · 4-((5-bromofuran-2-yl)methyl)-8-(2-chloroacetyl)-1-thia-4,8-diazaspiro[4.5]decan-3-one · ligand · 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	50	0.33	0.78	11	J3X

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

7EFX · Crystal Structure of human PIN1 complexed with covalent inhibitor · 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 Q13526
Elsewhere: RCSB PDB 7EFX · PDBe 7EFX · UniProt Q13526

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