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UniProt P63208

S-phase kinase-associated protein 1 (P63208)

S-phase kinase-associated protein 1 (UniProt P63208): 68 experimental structures on GenesisL1, 23 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P63208
Protein
S-phase kinase-associated protein 1
Experimental structures
68
Predicted models
0
Pockets
23 · 5 records with a druggable one

Structures

68 records of P63208 in the MolNFT archive: 68 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1FQVInsights into scf ubiquitin ligases from the structure of the skp1-skp2 complexx-ray diffractionB, D, F, H, J, L, N, P——
1FQVInsights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complexx-ray diffractionB, D, F, H, J, L, N, P——
1FS1Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complexx-ray diffractionB, D——
1FS1Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complexx-ray diffractionB, D——
1FS2Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complexx-ray diffractionB, D——
1FS2Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complexx-ray diffractionB, D——
1LDKStructure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complexx-ray diffractionD——
1LDKStructure of the CUL1-RBX1-SKP1-F BOXSKP2 scf ubiquitin ligase complexx-ray diffractionD——
1P22Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine…x-ray diffractionB——
1P22Structure of a beta-TRCP1-SKP1-beta-catenin complex: destruction motif binding and lysine…x-ray diffractionB——
2ASSCrystal structure of the Skp1-Skp2-Cks1 complexx-ray diffractionA——
2ASSCrystal structure of the SKP1-SKP2-CKS1 complexx-ray diffractionA——
2ASTCrystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptidex-ray diffractionA——
2ASTCrystal structure of SKP1-SKP2-CKS1 in complex with a P27 peptidex-ray diffractionA——
2E31Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligasex-ray diffractionB——
2E31Structural basis for selection of glycosylated substrate by SCFFBS1 ubiquitin ligasex-ray diffractionB——
2E32Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligasex-ray diffractionB, D——
2E32Structural basis for selection of glycosylated substrate by SCFFBS1 ubiquitin ligasex-ray diffractionB, D——
2OVPStructure of the Skp1-Fbw7 complexx-ray diffractionA——
2OVPStructure of the SKP1-FBW7 complexx-ray diffractionA——
2OVQStructure of the Skp1-Fbw7-CyclinEdegC complexx-ray diffractionA——
2OVQStructure of the SKP1-FBW7-cyclinedegc complexx-ray diffractionA——
2OVRStructure of the Skp1-Fbw7-CyclinEdegN complexx-ray diffractionA——
2OVRStructure of the SKP1-FBW7-cyclinedegn complexx-ray diffractionA——
3L2OStructure-Based Mechanism of Dimerization-Dependent Ubiquitination by the SCFFbx4 Ubiquitin Ligasex-ray diffractionA——
3L2OStructure-based mechanism of dimerization-dependent ubiquitination by the SCFFBX4 ubiquitin ligasex-ray diffractionA——
3WSOCrystal structure of the Skp1-FBG3 complexx-ray diffractionB——
3WSOCrystal structure of the SKP1-FBG3 complexx-ray diffractionB——
4I6JA ubiquitin ligase-substrate complexx-ray diffractionC——
4I6JA ubiquitin ligase-substrate complexx-ray diffractionC——
5IBKSkp1-F-box in complex with a ubiquitin variantx-ray diffractionA, D——
5IBKSKP1-F-box in complex with a ubiquitin variantx-ray diffractionA, D——
5JH5Structural basis for the hierarchical assembly of the core of PRC1.1x-ray diffractionB——
5K35Structure of the Legionella effector, AnkB, in complex with human Skp1x-ray diffractionB——
5K35Structure of the legionella effector, ankb, in complex with human SKP1x-ray diffractionB——
5V4BCrystal structure of the Skp1-FBXW7-DISC1 complexx-ray diffractionA—3 (best 0.80)
5V4BCrystal structure of the SKP1-FBXW7-DISC1 complexx-ray diffractionA——
5VZTCrystal structure of the SKP1-FBXO31 complexx-ray diffractionA, C——
5VZUCrystal structure of the SKP1-FBXO31-cyclin D1 complexx-ray diffractionA, C——
5XYLSolution structure of SKP1 from homo sapienssolution nmrA——
6BVAUbiquitin variant (UBV.FL10.1) bound to a human SKP1-FBL10 fragment complex.x-ray diffractionD, C——
6BYHUbiquitin Variant (UbV.Fl11.1) bound to a human Skp1-Fbl11 fragment complex.x-ray diffractionA, B, G—9 (best 0.60)
6BYHUbiquitin variant (UBV.FL11.1) bound to a human SKP1-FBL11 fragment complex.x-ray diffractionA, B, G——
6C16Ubiquitin variant (UbV.Fbl10.1) bound to a human Skp1-Fbl11 fragment complex.x-ray diffractionA, B——
6C16Ubiquitin variant (UBV.FBL10.1) bound to a human SKP1-FBL11 fragment complex.x-ray diffractionA, B——
6M90Monophosphorylated PSER33 B-catenin peptide, B-TRCP/SKP1, nrx-2776 ternary complexx-ray diffractionB——
6M91Monophosphorylated PSER33 B-catenin peptide, B-TRCP/SKP1, nrx-103094 ternary complexx-ray diffractionB——
6M92Monophosphorylated PSER33 B-catenin peptide, B-TRCP/SKP1, nrx-2663 ternary complexx-ray diffractionB——
6M93Monophosphorylated PSER33 B-catenin peptide, B-TRCP/SKP1, nrx-1933 ternary complexx-ray diffractionB——
6M94Monophosphorylated pSer33 b-Catenin peptide bound to b-TrCP/Skp1 Complexx-ray diffractionB——
6M94Monophosphorylated PSER33 B-catenin peptide bound to B-TRCP/SKP1 complexx-ray diffractionB——
6O60Crystal structure of GGTASE3-FBXL2-SKP1 complexx-ray diffractionD——
6TTUUbiquitin ligation to substrate by a cullin-ring E3 ligase at 3.7A resolution: NEDD8-CUL1-RBX1…electron microscopyS——
6VCDCryo-EM structure of IRP2-FBXL5-SKP1 complexelectron microscopyC——
6W66The structure of the F64A, S172A mutant KEAP1-btb domain in complex with SKP1-FBXL17x-ray diffractionA——
6WCQStructure of a substrate-bound dqc ubiquitin ligaseelectron microscopyA——
6WNXFBXW11-SKP1 in complex with a PSER33/PSER37 beta-catenin peptidex-ray diffractionB, E, H——
7B5LUbiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly…electron microscopyS——
7B5LUbiquitin ligation to F-box protein substrates by scf-rbr E3-E3 super- assembly…electron microscopyS——
7B5MUbiquitin ligation to F-box protein substrates by scf-rbr E3-E3 super- assembly…electron microscopyS——

8 records more on the page itself.

Elsewhere

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