1FQV: SKP2

Name: PDB 1FQV: 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 2.8 Å resolution. Released 29 Nov 2000.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 16
Atoms: 29,256
Mol. weight: 438.21 kDa
Released: 29 Nov 2000

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

Secondary structure: helices and β-sheets

1FQV contains 183 α-helices and 176 β-strands across 16 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: 14 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	126-132	7
α-helix	137-142	6
α-helix	146-148	3
β-strand	151-153	3	1
β-strand	158	1	2
α-helix	161-168	8
β-strand	174-176	3	1
β-strand	181-182	2	2
β-strand	193	1	3
β-strand	197-199	3	1
β-strand	204-205	2	2
α-helix	207-214	8
β-strand	217	1	3
β-strand	222-224	3	1
β-strand	229	1	4
α-helix	232-239	8
β-strand	246-248	3	1
β-strand	253	1	4
α-helix	257-266	10
β-strand	272-274	3	1
α-helix	283-292	10
β-strand	299-301	3	1
α-helix	311-320	10
β-strand	326-328	3	1
α-helix	337-339	3
α-helix	340-343	4
β-strand	351-353	3	1
α-helix	363-370	8
β-strand	376-378	3	1
α-helix	385-394	10
β-strand	400	1	1
β-strand	421	1	5
β-strand	424	1	5
β-strand	428-429	2	1

Chains B, H and L: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	6
β-strand	13-17	5	6
α-helix	18-21	4
α-helix	25-33	9
β-strand	45-47	3	6
α-helix	52-64	13
α-helix	87-92	6
α-helix	97-109	13
α-helix	113-127	15
α-helix	132-139	8
α-helix	149-155	7

Chain C: 16 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	126-132	7
α-helix	137-142	6
α-helix	146-149	4
β-strand	151-153	3	7
β-strand	158	1	8
α-helix	161-168	8
β-strand	174-176	3	7
β-strand	181-182	2	8
α-helix	192-193	2
β-strand	197-199	3	7
β-strand	204-205	2	8
α-helix	207-214	8
β-strand	222-224	3	7
β-strand	229	1	9
α-helix	232-238	7
β-strand	246-248	3	7
β-strand	253	1	9
α-helix	257-266	10
β-strand	272-274	3	7
α-helix	283-292	10
β-strand	299-301	3	7
α-helix	311-320	10
β-strand	326-328	3	7
α-helix	337-339	3
α-helix	340-343	4
β-strand	351-353	3	7
α-helix	362-370	9
β-strand	376-378	3	7
α-helix	385-394	10
β-strand	399-400	2	7
α-helix	421-423	3
β-strand	428	1	7

Chain D: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	10
β-strand	13-17	5	10
α-helix	18-21	4
α-helix	25-33	9
β-strand	44-46	3	10
α-helix	52-64	13
α-helix	87-92	6
α-helix	97-109	13
α-helix	113-127	15
α-helix	132-139	8
α-helix	149-155	7

Chain E: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	126-132	7
α-helix	137-142	6
α-helix	146-148	3
β-strand	151-153	3	11
β-strand	158	1	12
α-helix	161-168	8
β-strand	174-176	3	11
β-strand	181-182	2	12
α-helix	192-193	2
β-strand	197-199	3	11
β-strand	204-205	2	12
α-helix	207-214	8
β-strand	222-224	3	11
β-strand	229	1	13
α-helix	232-238	7
β-strand	246-248	3	11
β-strand	253	1	13
α-helix	257-266	10
β-strand	272-274	3	11
α-helix	283-292	10
β-strand	299-301	3	11
α-helix	311-320	10
β-strand	326-328	3	11
α-helix	337-339	3
α-helix	340-343	4
β-strand	351-353	3	11
α-helix	362-369	8
β-strand	376-378	3	11
α-helix	385-394	10
β-strand	400	1	11
β-strand	421	1	14
β-strand	424	1	14
β-strand	428-429	2	11

Chain F: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	15
β-strand	13-17	5	15
α-helix	18-21	4
α-helix	25-33	9
β-strand	45-47	3	15
α-helix	52-64	13
α-helix	87-92	6
α-helix	97-109	13
α-helix	113-127	15
α-helix	132-138	7
α-helix	149-155	7

Chain G: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	126-132	7
α-helix	137-142	6
α-helix	146-149	4
β-strand	151-153	3	16
β-strand	158	1	17
α-helix	161-168	8
β-strand	174-176	3	16
β-strand	181-182	2	17
α-helix	192-193	2
β-strand	197-199	3	16
β-strand	204-205	2	17
α-helix	207-214	8
β-strand	222-224	3	16
β-strand	229	1	18
α-helix	232-238	7
β-strand	246-248	3	16
β-strand	253	1	18
α-helix	257-266	10
β-strand	272-274	3	16
α-helix	283-292	10
β-strand	299-301	3	16
α-helix	311-320	10
β-strand	326-328	3	16
α-helix	337-339	3
α-helix	340-343	4
β-strand	351-353	3	16
α-helix	362-370	9
β-strand	376-378	3	16
α-helix	385-394	10
β-strand	400	1	16
β-strand	421	1	19
β-strand	424	1	19
β-strand	428-429	2	16

Chain I: 14 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	126-132	7
α-helix	137-142	6
α-helix	146-149	4
β-strand	151-153	3	21
β-strand	158	1	22
α-helix	161-168	8
β-strand	174-176	3	21
β-strand	181-182	2	22
β-strand	197-199	3	21
β-strand	204-205	2	22
α-helix	207-214	8
β-strand	222-224	3	21
β-strand	229	1	23
α-helix	232-238	7
β-strand	246-248	3	21
β-strand	253	1	23
α-helix	257-266	10
β-strand	272-274	3	21
α-helix	283-292	10
β-strand	299-301	3	21
α-helix	311-320	10
β-strand	326-328	3	21
α-helix	337-339	3
α-helix	340-343	4
β-strand	351-353	3	21
α-helix	362-369	8
β-strand	376-378	3	21
α-helix	385-394	10
β-strand	400	1	21
β-strand	421	1	24
β-strand	424	1	24
β-strand	428-429	2	21

6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SKP2	A, C, E, G, I, K, M, O	protein	336	Homo sapiens	Q13309 (AlphaFold model)
SKP1	B, D, F, H, J, L, N, P	protein	149	Homo sapiens	P63208 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K, M, O), FASTA

>1FQV_1 SKP2 (chains A, C, E, G, I, K, M, O)
RENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLH
PDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKL
QNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFD
FTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCF
QEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQI
NCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL

Sequence of entity 2 (B, D, F, H, J, L, N, P), FASTA

>1FQV_2 SKP1 (chains B, D, F, H, J, L, N, P)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDPVPLPNVNAAILKKVIQWCTHHK
DDPGGSGTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKTPEE
IRKTFNIKNDFTEEEEAQVRKENQWCEEK

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:

1FS1 1.8 Å, Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complex
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
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

Browse structure collections

About this viewer

MolViewer shows 1FQV 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.