4N1M: Cyclophilin A

Structure of Cyclophilin A in complex with GlyPro. Determined by X-ray diffraction at 1.15 Å resolution. Released 12 Aug 2015.

Method
X-ray diffraction
Resolution
1.15 Å
Organism
Homo sapiens
Chains
1
Atoms
1,577
Mol. weight
18.58 kDa
Ligands
GLY, PRO
Released
12 Aug 2015

Explore 4N1M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N1M contains 4 α-helices and 13 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: 4 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix-1-46
β-strand5-1281
β-strand15-24101
α-helix30-4112
β-strand5211
β-strand55-5731
β-strand61-6441
β-strand77-7822
β-strand8012
β-strand8313
β-strand97-10041
β-strand10813
β-strand112-11541
α-helix120-1223
β-strand128-13471
α-helix136-1438
β-strand156-16491

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase AAprotein168Homo sapiensP62937 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4N1M_1 Peptidyl-prolyl cis-trans isomerase A (chains A)
SHMMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRII
PGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTA
KTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE

Ligands and cofactors

IDNameFormulaCopies
GLYGlycineC2 H5 N O21
PROProlineC5 H9 N O21

Primary citation

Mapping the binding surface of Cyclophilin A. Mcnae, I.W., Dornan, D., Patterson, A.F. et al. To be published.

Other PDB entries of the same protein (UniProt P62937 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 4N1M 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.