3K3K

Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1) with ABA-bound closed-lid and ABA-free open-lid subunits

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004864	molecular_function	protein phosphatase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005773	cellular_component	vacuole
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0009705	cellular_component	plant-type vacuole membrane
A	0009738	biological_process	abscisic acid-activated signaling pathway
A	0010427	molecular_function	abscisic acid binding
A	0038023	molecular_function	signaling receptor activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0044389	molecular_function	ubiquitin-like protein ligase binding
A	0062049	cellular_component	protein phosphatase inhibitor complex
A	0080163	biological_process	regulation of protein serine/threonine phosphatase activity
A	1902584	biological_process	positive regulation of response to water deprivation
B	0004864	molecular_function	protein phosphatase inhibitor activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005773	cellular_component	vacuole
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0009705	cellular_component	plant-type vacuole membrane
B	0009738	biological_process	abscisic acid-activated signaling pathway
B	0010427	molecular_function	abscisic acid binding
B	0038023	molecular_function	signaling receptor activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0044389	molecular_function	ubiquitin-like protein ligase binding
B	0062049	cellular_component	protein phosphatase inhibitor complex
B	0080163	biological_process	regulation of protein serine/threonine phosphatase activity
B	1902584	biological_process	positive regulation of response to water deprivation

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE A8S B 1001

Chain	Residue
B	LYS59
B	PHE159
B	VAL163
B	HOH200
B	HOH214
B	HOH220
B	HOH221
B	HOH297
B	VAL83
B	PRO88
B	ALA89
B	SER92
B	PHE108
B	ILE110
B	LEU117
B	TYR120

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:19898494, ECO:0000269|PubMed:19933100

Chain	Residue	Details
A	LYS59
A	ALA89
A	ARG116
A	GLU141
B	LYS59
B	ALA89
B	ARG116
B	GLU141

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site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Involved in interactions with PP2Cs => ECO:0000269|PubMed:19407142

Chain	Residue	Details
A	PRO88
A	SER152
B	PRO88
B	SER152

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by CARK1 => ECO:0000269|PubMed:29928509

Chain	Residue	Details
A	THR78
B	THR78

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