7UXM: PPIA

Structure of PPIA in complex with FP29092, a Helicon Polypeptide. Determined by X-ray diffraction at 1.2 Å resolution. Released 28 Dec 2022.

Method: X-ray diffraction
Resolution: 1.2 Å
Organisms: Homo sapiens, synthetic construct
Chains: 6
Atoms: 5,172
Mol. weight: 61.85 kDa
Ligands: NH2, WHL
Released: 28 Dec 2022

Explore 7UXM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UXM contains 14 α-helices and 30 β-strands across 6 chains. 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
α-helix	1-4	4
β-strand	5-12	8	1
β-strand	15-24	10	1
α-helix	30-41	12
β-strand	52-57	6	1
β-strand	61-64	4	1
β-strand	83	1	2
β-strand	97-100	4	1
β-strand	108	1	2
β-strand	112-115	4	1
α-helix	120-122	3
β-strand	128-132	5	1
α-helix	136-142	7
α-helix	143-145	3
β-strand	156-163	8	1

Chain B: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	3
β-strand	15-24	10	3
α-helix	30-41	12
β-strand	52-57	6	3
β-strand	61-64	4	3
β-strand	83	1	4
β-strand	97-100	4	3
β-strand	108	1	4
β-strand	112-115	4	3
α-helix	120-122	3
β-strand	128-134	7	3
α-helix	136-143	8
β-strand	156-163	8	3

Chain C: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	5
β-strand	15-24	10	5
α-helix	30-41	12
β-strand	52-57	6	5
β-strand	61-64	4	5
β-strand	83	1	6
β-strand	97-100	4	5
β-strand	108	1	6
β-strand	112-115	4	5
α-helix	120-122	3
β-strand	128-132	5	5
α-helix	136-143	8
β-strand	156-163	8	5

Chains D, E and F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-16	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase A	A, B, C	protein	166	Homo sapiens	P62937 (AlphaFold model)
FP29092	D, E, F	protein	18	synthetic construct

Sequence of entity 1 (A, B, C), FASTA

>7UXM_1 Peptidyl-prolyl cis-trans isomerase A (chains A, B, C)
GMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPG
FMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKT
EWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE

Sequence of entity 2 (D, E, F), FASTA

>7UXM_2 FP29092 (chains D, E, F)
XDPANQDCHVAAWHCWQR

Ligands and cofactors

ID	Name	Formula	Copies
NH2	Amino group	H2 N	3
WHL	N,N'-(1,4-phenylene)diacetamide	C10 H12 N2 O2	3

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

Primary citation

De novo mapping of alpha-helix recognition sites on protein surfaces using unbiased libraries. Li, K., Tokareva, O.S., Thomson, T.M. et al. Proc Natl Acad Sci U S A (2022) 119:e2210435119-e2210435119. DOI 10.1073/pnas.2210435119 · PubMed

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

9E3S 1.08 Å, Tricomplex of RMC-9945, KRAS G12N, and CypA
9BG4 1.14 Å, Tri-complex of Compound-2, KRAS G12V, and CypA
4N1M 1.15 Å, Structure of Cyclophilin A in complex with GlyPro.
5F66 1.15 Å, High-resolution isotropic multiconformer synchrotron model of CypA at 273 K
9GHY 1.15 Å, Cyclophilin A in complex with Sanglifehrin A analogue (2R,3S,7S,10S,E)-10-(3-aminopropyl)…
6GJL 1.16 Å, Cyclophilin A complexed with tri-vector ligand 10.
6GS6 1.16 Å, Cyclophilin A single mutant D66A in complex with an inhibitor.
2X25 1.2 Å, Free acetyl-CypA orthorhombic form
4YUO 1.2 Å, High-resolution multiconformer synchrotron model of CypA at 273 K
8TBG 1.2 Å, Tricomplex of RMC-7977, HRAS WT, and CypA
9BFV 1.2 Å, Tri-complex of Compound-23, KRAS G12C, and CypA
9BFW 1.2 Å, Tri-complex of Compound-4, KRAS G12C, and CypA

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