1PIN: Peptidyl-prolyl cis-trans isomerase

Name: PDB 1PIN: PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens
Published: 1998-10-14
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens. Determined by X-ray diffraction at 1.35 Å resolution. Released 14 Oct 1998.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,458
Mol. weight: 19.08 kDa
Ligands: 1PG, PRO, ALA
Released: 14 Oct 1998

Explore 1PIN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PIN contains 5 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	1
β-strand	22-26	5	1
β-strand	32-33	2	1
β-strand	55-62	8	2
β-strand	72	1	3
β-strand	75	1	3
α-helix	82-98	17
α-helix	103-110	8
α-helix	114-118	5
β-strand	121-125	5	2
α-helix	132-140	9
α-helix	141-142	2
β-strand	146	1	2
β-strand	150-151	2	2
β-strand	156-161	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase	A	protein	163	Homo sapiens	Q13526 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1PIN_1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (chains A)
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHL
LVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARG
DLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE

Ligands and cofactors

ID	Name	Formula	Copies
1PG	2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol	C11 H24 O6	2
PRO	Proline	C5 H9 N O2	1
ALA	Alanine	C3 H7 N O2	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Ranganathan, R., Lu, K.P., Hunter, T. et al. Cell (1997) 89:875-886. DOI 10.1016/S0092-8674(00)80273-1 · PubMed

Other PDB entries of the same protein (UniProt Q13526 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7AZ2 1.08 Å, 14-3-3 sigma with Pin1 binding site pS72 and covalently bound LvD1014
7AZ1 1.15 Å, 14-3-3 sigma with Pin1 binding site pS72 and covalently bound LvD1013
3I6C 1.3 Å, Structure-Based Design of Novel PIN1 Inhibitors (II)
4TNS 1.33 Å, Structure of Pin1 PPIase domain bound with all-trans retinoic acid
3TC5 1.4 Å, Selective targeting of disease-relevant protein binding domains by O-phosphorylated…
7AXN 1.4 Å, 14-3-3 sigma in complex with Pin1 binding site pS72 and covalently bound TCF521-026
7BG3 1.4 Å, 14-3-3 sigma with Pin1 binding site pS72 and covalently bound PC2046
6VAJ 1.42 Å, Crystal Structure Analysis of human PIN1
9KFZ 1.43 Å, Crystal structure of the PIN1 and fragment 59 complex
2ITK 1.45 Å, human Pin1 bound to D-PEPTIDE
2ZQT 1.46 Å, Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
2F21 1.5 Å, human Pin1 Fip mutant

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