4KRC

Crystal Structure of Pho85-Pcl10-ATP-gamma-S Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000278	biological_process	mitotic cell cycle
A	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
A	0001676	biological_process	long-chain fatty acid metabolic process
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004693	molecular_function	cyclin-dependent protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005935	cellular_component	cellular bud neck
A	0005979	biological_process	regulation of glycogen biosynthetic process
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006468	biological_process	protein phosphorylation
A	0006974	biological_process	DNA damage response
A	0009891	biological_process	positive regulation of biosynthetic process
A	0016239	biological_process	positive regulation of macroautophagy
A	0016242	biological_process	negative regulation of macroautophagy
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019216	biological_process	regulation of lipid metabolic process
A	0030952	biological_process	establishment or maintenance of cytoskeleton polarity
A	0031505	biological_process	fungal-type cell wall organization
A	0031647	biological_process	regulation of protein stability
A	0031648	biological_process	protein destabilization
A	0032878	biological_process	regulation of establishment or maintenance of cell polarity
A	0032880	biological_process	regulation of protein localization
A	0044843	biological_process	cell cycle G1/S phase transition
A	0045719	biological_process	negative regulation of glycogen biosynthetic process
A	0045936	biological_process	negative regulation of phosphate metabolic process
A	0046822	biological_process	regulation of nucleocytoplasmic transport
A	0050849	biological_process	negative regulation of calcium-mediated signaling
A	0051302	biological_process	regulation of cell division
A	0051726	biological_process	regulation of cell cycle
A	0055088	biological_process	lipid homeostasis
A	0071073	biological_process	positive regulation of phospholipid biosynthetic process
A	0106310	molecular_function	protein serine kinase activity
A	1901987	biological_process	regulation of cell cycle phase transition
A	1990860	cellular_component	Pho85-Pho80 CDK-cyclin complex
B	0000079	biological_process	regulation of cyclin-dependent protein serine/threonine kinase activity
B	0019901	molecular_function	protein kinase binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASN138
A	ASP151
A	AGS402

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site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE AGS A 402

Chain	Residue
A	GLU83
A	MET85
A	ASP88
A	ASP133
A	LYS135
A	GLN137
A	ASN138
A	LEU140
A	ASP151
A	MG401
A	HOH504
A	GLY16
A	THR17
A	TYR18
A	VAL21
A	ALA34
A	LYS36

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGNGTYATVYkGlnkttgvy..........VALK

Chain	Residue	Details
A	LEU13-LYS36

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpqNLLI

Chain	Residue	Details
A	ILE129-ILE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Not phosphorylated","evidences":[{"source":"PubMed","id":"10490639","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"10620010","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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