3UJG

Crystal structure of SnRK2.6 in complex with HAB1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	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	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005985	biological_process	sucrose metabolic process
A	0006468	biological_process	protein phosphorylation
A	0006636	biological_process	unsaturated fatty acid biosynthetic process
A	0006952	biological_process	defense response
A	0006970	biological_process	response to osmotic stress
A	0009414	biological_process	response to water deprivation
A	0009651	biological_process	response to salt stress
A	0009737	biological_process	response to abscisic acid
A	0009738	biological_process	abscisic acid-activated signaling pathway
A	0009789	biological_process	positive regulation of abscisic acid-activated signaling pathway
A	0009931	molecular_function	calcium-dependent protein serine/threonine kinase activity
A	0010118	biological_process	stomatal movement
A	0010119	biological_process	regulation of stomatal movement
A	0010359	biological_process	obsolete regulation of anion channel activity
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019432	biological_process	triglyceride biosynthetic process
A	0019903	molecular_function	protein phosphatase binding
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0046777	biological_process	protein autophosphorylation
A	0048366	biological_process	leaf development
A	0071244	biological_process	cellular response to carbon dioxide
A	0071485	biological_process	cellular response to absence of light
A	0090333	biological_process	regulation of stomatal closure
A	0106310	molecular_function	protein serine kinase activity
A	1902456	biological_process	regulation of stomatal opening
A	2000377	biological_process	regulation of reactive oxygen species metabolic process
B	0004722	molecular_function	protein serine/threonine phosphatase activity
B	0006470	biological_process	protein dephosphorylation
B	0043169	molecular_function	cation binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 363

Chain	Residue
A	ARG139
A	LYS142
B	GLN384
B	TRP385
B	GLN386
B	GLY387

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 364

Chain	Residue
B	ARG199
B	GLY244
B	HIS245
A	LYS174
A	SER175
A	THR176

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 100

Chain	Residue
B	ASP204
B	ASP243
B	GLY244
B	MG512

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 512

Chain	Residue
B	MG100
B	ASP243
B	ASP432
B	ASP492

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 513

Chain	Residue
A	LYS174
B	ARG199
B	SER200

---

Functional Information from PROSITE/UniProt

site_id	PS01032
Number of Residues	9
Details	PPM_1 PPM-type phosphatase domain signature. FFGVYDGHG

Chain	Residue	Details
B	PHE238-GLY246

---

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

Chain	Residue	Details
A	ILE27-LYS50

---

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

Chain	Residue	Details
A	VAL136-LEU148

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	26
Details	Region: {"description":"Activation loop","evidences":[{"source":"PubMed","id":"16766677","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"16766677","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16766677","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21658606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QN1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LA7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LGA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WVO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KB3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Lock"}

Chain

Residue

Details

---