MolNFT v1 · #146852 · protein

Crystal structure analysis of PIN1

6DUN · Peptidyl-prolyl cis-trans isomerase nima-interacting 1: “Crystal structure analysis of PIN1”. X-ray diffraction, 1 ligand (TAS), 2 pockets (best druggability 0.45). MolNFT v1 #146852 on GenesisL1: 3D structure, binding sites and…

PDB: 6DUN
Type: protein
Length: 229 residues
Chains: 2
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: TAS
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 34% 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	115	33% helix, 23% strand	Q13526
B	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	114	34% helix, 25% strand	Q13526

Ligands and binding sites

TAS · Trihydroxyarsenite(iii) · ligand · 2 copies · chains A, B

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	131	0.45	0.77	20	empty
2	73	0.34	0.76	17	TAS

Interfaces

1 interface between chains.

A–B · 350 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6DUN · Crystal Structure Analysis of 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 6DUN · PDBe 6DUN · UniProt Q13526

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