5JO1

Crystal structure of phaseic 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	5
Details	binding site for residue MG B 601

Chain	Residue
B	ASP243
B	ASP432
B	ASP492
B	MG602
B	HOH710

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site_id	AC2
Number of Residues	5
Details	binding site for residue MG B 602

Chain	Residue
B	HOH710
B	ASP243
B	GLY244
B	MG601
B	HOH706

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site_id	AC3
Number of Residues	12
Details	binding site for residue 6LM A 800

Chain	Residue
A	LYS79
A	VAL107
A	SER116
A	GLU118
A	PHE132
A	HIS139
A	LEU141
A	TYR144
A	PHE188
A	ASN196
A	HOH903
A	HOH913

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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	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22579247, ECO:0000269|PubMed:23844015, ECO:0007744|PDB:4DS8, ECO:0007744|PDB:4DSB, ECO:0007744|PDB:4DSC, ECO:0007744|PDB:4JDA

Chain	Residue	Details
B	ASP432
A	LYS79
B	ASP492

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O49686

Chain	Residue	Details
A	GLU170
A	ALA113

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22579247, ECO:0007744|PDB:4DSC

Chain	Residue	Details
A	ARG140

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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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