5JO2

Crystal structure of abscisic acid-bound abscisic acid receptor PYL3 in complex with type 2C protein phosphatase HAB1

Functional Information from GO Data

Chain	GOid	namespace	contents
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	14
Details	binding site for residue A8S A 800

Chain	Residue
A	LYS79
A	PHE188
A	VAL192
A	ASN196
A	HOH902
A	HOH903
A	PHE81
A	VAL107
A	ALA113
A	SER116
A	PHE132
A	HIS139
A	TYR144
A	GLU170

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG B 601

Chain	Residue
B	ASP243
B	ASP432
B	ASP492
B	MG602
B	HOH703
B	HOH706

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site_id	AC3
Number of Residues	4
Details	binding site for residue MG B 602

Chain	Residue
B	ASP243
B	GLY244
B	MG601
B	HOH707

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:21658606, ECO:0007744|PDB:3NMT, ECO:0007744|PDB:3QN1, ECO:0007744|PDB:3RT0, ECO:0007744|PDB:3UJG, ECO:0007744|PDB:3ZVU, ECO:0007744|PDB:4LA7, ECO:0007744|PDB:4LG5, ECO:0007744|PDB:4LGA, ECO:0007744|PDB:4WVO

Chain	Residue	Details
B	ASP243
B	ASP432
B	ASP492

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:19898420, ECO:0007744|PDB:3KB3

Chain	Residue	Details
A	GLU170
B	GLY244

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Lock

Chain	Residue	Details
B	TRP385

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686

Chain	Residue	Details
A	THR181
A	PRO112

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7

Chain	Residue	Details
A	VAL189

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Involved in the cis- to trans-homodimer conformation in the presence of ABA => ECO:0000269|PubMed:22579247

Chain	Residue	Details
A	SER195

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