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Human PIN1 bound to L-peptide

Analyse Human PIN1 bound to L-peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q5A
Type: protein
Length: 150 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase nima-interacting 1; Five residue peptide
EC: 5.2.1.8
UniProt: Q13526
Ligands: 16P, NH2
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 26% 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
B	Five residue peptide	protein	5	0% helix, 20% strand	—

Ligands and binding sites

16P · 3,6,9,12,15,18-hexaoxaicosane · ligand · chains A
NH2 · Amino group · ion · chains B

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	76	0.31	0.73	17	16P

Interfaces

1 interface between chains.

A–B · 419 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (nonstandard, phosphorylation).

Compared structures

2Q5A · human Pin1 bound to L-PEPTIDE · 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 2Q5A · PDBe 2Q5A · UniProt Q13526

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