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Crystal structure analysis of human PIN1

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

PDB: 6VAJ
Type: protein
Length: 150 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: QT7, SO4
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 26% 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	150	26% helix, 24% strand	Q13526

Ligands and binding sites

QT7 · 2-chloro-N-(2,2-dimethylpropyl)-N-[(3R)-1,1-dioxo-1lambda~6~-thiolan-3-yl]acetamide · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
PG4 · Tetraethylene glycol · 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	56	0.29	0.75	17	empty

Modifications

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

Compared structures

6VAJ · Crystal Structure Analysis of human PIN1 · 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 6VAJ · PDBe 6VAJ · UniProt Q13526

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