3TC5: PDB entry 3TC5

Selective targeting of disease-relevant protein binding domains by O-phosphorylated natural product derivatives. Determined by X-ray diffraction at 1.4 Å resolution. Released 31 Aug 2011.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,452
Mol. weight: 19.22 kDa
Ligands: 3T5
Released: 31 Aug 2011

Explore 3TC5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TC5 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	142	1
β-strand	146	1	2
β-strand	150-152	3	2
β-strand	155-161	7	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1	A	protein	166	Homo sapiens	Q13526 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3TC5_1 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (chains A)
GSHMADEEKLPPGWEKAMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRC
SHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAK
ARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE

Ligands and cofactors

ID	Name	Formula	Copies
3T5	(11alpha,16alpha)-9-fluoro-11,17-dihydroxy-16-methyl-3,20-dioxopregna-1,4-dien-…	C22 H30 F O8 P	1

Water and common crystallization additives (P6G) are not listed.

Primary citation

Selective targeting of disease-relevant protein binding domains by o-phosphorylated natural product derivatives. Graber, M., Janczyk, W., Sperl, B. et al. ACS Chem Biol (2011) 6:1008-1014. DOI 10.1021/cb2001796 · 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
1PIN 1.35 Å, PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens
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

Browse structure collections

About this viewer

MolViewer shows 3TC5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.