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Structure-guided design of alpha-amino acid-derived PIN1 inhibitors

Analyse Structure-guided design of alpha-amino acid-derived PIN1 inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KAG
Type: protein
Length: 145 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: 4D7
Pockets: 2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	145	27% helix, 28% strand	Q13526

Ligands and binding sites

4D7 · 3-(1H-benzimidazol-2-yl)-N-[(2-methylfuran-3-yl)carbonyl]-D-alanine · ligand · chains A
12P · Dodecaethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.32	0.76	16	4D7
2	59	0.29	0.74	15	12P

Compared structures

3KAG · Structure-guided design of alpha-amino acid-derived Pin1 inhibitors · 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 3KAG · PDBe 3KAG · UniProt Q13526

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