1FS1: Cyclin A/CDK2-associated P19

Name: PDB 1FS1: Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complex
Published: 2000-11-29
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 29 Nov 2000.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,067
Mol. weight: 44.24 kDa
Released: 29 Nov 2000

Explore 1FS1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FS1 contains 25 α-helices and 6 β-strands across 4 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, 0 β-strands

Element	Residues	Length
α-helix	114-121	8
α-helix	126-128	3
α-helix	129-133	5
α-helix	137-143	7
α-helix	146-148	3

Chain B: 7 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	13-17	5	1
α-helix	18-22	5
α-helix	25-33	9
β-strand	45-46	2	1
α-helix	52-65	14
α-helix	87-92	6
α-helix	97-110	14
α-helix	113-127	15
α-helix	132-138	7

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	114-122	9
α-helix	126-128	3
α-helix	129-133	5
α-helix	137-143	7
α-helix	146-148	3

Chain D: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	2
β-strand	13-17	5	2
α-helix	18-21	4
α-helix	25-29	5
α-helix	30-34	5
β-strand	45-46	2	2
α-helix	52-65	14
α-helix	87-92	6
α-helix	97-110	14
α-helix	113-125	13
α-helix	132-139	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclin A/CDK2-associated P19	A, C	protein	53	Homo sapiens	Q13309 (AlphaFold model)
Cyclin A/CDK2-associated P45	B, D	protein	141	Homo sapiens	P63208 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1FS1_1 CYCLIN A/CDK2-ASSOCIATED P19 (chains A, C)
RENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLD

Sequence of entity 2 (B, D), FASTA

>1FS1_2 CYCLIN A/CDK2-ASSOCIATED P45 (chains B, D)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDPVPLPNVNAAILKKVIQWCTHHK
DDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANM
IKGKTPEEIRKTFNIKNDFTE

Primary citation

Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Schulman, B.A., Carrano, A.C., Jeffrey, P.D. et al. Nature (2000) 408:381-386. DOI 10.1038/35042620 · PubMed

Other PDB entries of the same protein (UniProt Q13309 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2AST 2.3 Å, Crystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptide
7Z8V 2.7 Å, CAND1-SCF-SKP2 (SKP1deldel) CAND1 engaged SCF rocked
1FQV 2.8 Å, Insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
1FS2 2.9 Å, Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complex
8OR3 2.9 Å, CAND1-CUL1-RBX1-SKP1-SKP2-DCNL1
9QO4 2.95 Å, Dissociation-state-3 of 9-subunit CSN and SCF (SKP1-SKP2-CKS1) complex
2ASS 3.0 Å, Crystal structure of the Skp1-Skp2-Cks1 complex
7Z8T 3.0 Å, CAND1-SCF-SKP2 CAND1 engaged SCF rocked
1LDK 3.1 Å, Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
7ZBZ 3.1 Å, CAND1 delhairpin-SCF-SKP2 CAND1 partly engaged SCF partly rocked
8OR0 3.1 Å, CAND1-CUL1-RBX1-SKP1-SKP2-CKS1-CDK2
7LUO 3.17 Å, N-terminus of Skp2 bound to Cyclin A

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