5VZT

Crystal structure of the Skp1-FBXO31 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000209	biological_process	protein polyubiquitination
A	0000785	cellular_component	chromatin
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006879	biological_process	intracellular iron ion homeostasis
A	0007346	biological_process	regulation of mitotic cell cycle
A	0008013	molecular_function	beta-catenin binding
A	0010564	biological_process	regulation of cell cycle process
A	0010824	biological_process	regulation of centrosome duplication
A	0014033	biological_process	neural crest cell differentiation
A	0016567	biological_process	protein ubiquitination
A	0019005	cellular_component	SCF ubiquitin ligase complex
A	0019904	molecular_function	protein domain specific binding
A	0030510	biological_process	regulation of BMP signaling pathway
A	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
A	0031507	biological_process	heterochromatin formation
A	0031519	cellular_component	PcG protein complex
A	0032006	biological_process	regulation of TOR signaling
A	0042752	biological_process	regulation of circadian rhythm
A	0042981	biological_process	regulation of apoptotic process
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0050727	biological_process	regulation of inflammatory response
A	0051124	biological_process	synaptic assembly at neuromuscular junction
A	0051298	biological_process	centrosome duplication
A	0051457	biological_process	maintenance of protein location in nucleus
A	0051726	biological_process	regulation of cell cycle
A	0060173	biological_process	limb development
A	0060271	biological_process	cilium assembly
A	0070936	biological_process	protein K48-linked ubiquitination
A	0097602	molecular_function	cullin family protein binding
A	0140677	molecular_function	molecular function activator activity
A	0160072	molecular_function	ubiquitin ligase complex scaffold activity
A	1901524	biological_process	regulation of mitophagy
A	1904415	biological_process	regulation of xenophagy
A	1990444	molecular_function	F-box domain binding
A	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
A	1990757	molecular_function	ubiquitin ligase activator activity
A	2000001	biological_process	regulation of DNA damage checkpoint
C	0000082	biological_process	G1/S transition of mitotic cell cycle
C	0000209	biological_process	protein polyubiquitination
C	0000785	cellular_component	chromatin
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0006338	biological_process	chromatin remodeling
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0006879	biological_process	intracellular iron ion homeostasis
C	0007346	biological_process	regulation of mitotic cell cycle
C	0008013	molecular_function	beta-catenin binding
C	0010564	biological_process	regulation of cell cycle process
C	0010824	biological_process	regulation of centrosome duplication
C	0014033	biological_process	neural crest cell differentiation
C	0016567	biological_process	protein ubiquitination
C	0019005	cellular_component	SCF ubiquitin ligase complex
C	0019904	molecular_function	protein domain specific binding
C	0030510	biological_process	regulation of BMP signaling pathway
C	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
C	0031507	biological_process	heterochromatin formation
C	0031519	cellular_component	PcG protein complex
C	0032006	biological_process	regulation of TOR signaling
C	0042752	biological_process	regulation of circadian rhythm
C	0042981	biological_process	regulation of apoptotic process
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0050727	biological_process	regulation of inflammatory response
C	0051124	biological_process	synaptic assembly at neuromuscular junction
C	0051298	biological_process	centrosome duplication
C	0051457	biological_process	maintenance of protein location in nucleus
C	0051726	biological_process	regulation of cell cycle
C	0060173	biological_process	limb development
C	0060271	biological_process	cilium assembly
C	0070936	biological_process	protein K48-linked ubiquitination
C	0097602	molecular_function	cullin family protein binding
C	0140677	molecular_function	molecular function activator activity
C	0160072	molecular_function	ubiquitin ligase complex scaffold activity
C	1901524	biological_process	regulation of mitophagy
C	1904415	biological_process	regulation of xenophagy
C	1990444	molecular_function	F-box domain binding
C	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
C	1990757	molecular_function	ubiquitin ligase activator activity
C	2000001	biological_process	regulation of DNA damage checkpoint

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN B 601

Chain	Residue
B	CYS206
B	TYR208
B	HIS214
B	CYS230
B	HIS236

---

site_id	AC2
Number of Residues	10
Details	binding site for residue DTT B 602

Chain	Residue
B	ILE337
B	LEU472
B	ILE473
B	ALA474
B	TRP500
B	LEU503
B	HIS312
B	LYS330
B	ASP334
B	ASN336

---

site_id	AC3
Number of Residues	2
Details	binding site for residue PO4 B 603

Chain	Residue
B	ASP528
B	LEU531

---

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 B 604

Chain	Residue
B	ARG242
B	GLN279
D	GLU268

---

site_id	AC5
Number of Residues	3
Details	binding site for residue PO4 B 605

Chain	Residue
B	ARG242
B	PHE246
D	GLU268

---

site_id	AC6
Number of Residues	1
Details	binding site for residue PO4 B 606

Chain	Residue
B	ILE170

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 601

Chain	Residue
D	CYS206
D	HIS214
D	CYS230
D	HIS236

---

site_id	AC8
Number of Residues	8
Details	binding site for residue DTT D 602

Chain	Residue
D	TYR309
D	HIS312
D	LYS330
D	ASP334
D	ILE337
D	ILE473
D	ALA474
D	TRP500

---

site_id	AC9
Number of Residues	3
Details	binding site for residue PO4 D 603

Chain	Residue
B	LEU271
D	GLN243
D	LEU271

---

site_id	AD1
Number of Residues	4
Details	binding site for residue PO4 D 604

Chain	Residue
C	ASP1033
D	HIS195
D	MET197
D	THR203

---

site_id	AD2
Number of Residues	3
Details	binding site for residue PO4 D 605

Chain	Residue
D	PHE168
D	ILE170
D	ARG193

---

site_id	AD3
Number of Residues	2
Details	binding site for residue PO4 D 606

Chain	Residue
B	GLU268
D	ARG242

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	118
Details	Region: {"description":"Interaction with the F-box domain of F-box proteins","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Motif: {"description":"DDL motif","evidences":[{"source":"PubMed","id":"31413110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29279382","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VZT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5VZU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"19412162","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30171069","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---