4N0G

Crystal Structure of PYL13-PP2CA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0043169	molecular_function	cation binding
B	0004722	molecular_function	protein serine/threonine phosphatase activity
B	0006470	biological_process	protein dephosphorylation
B	0043169	molecular_function	cation binding
C	0004864	molecular_function	protein phosphatase inhibitor activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0009738	biological_process	abscisic acid-activated signaling pathway
C	0010427	molecular_function	abscisic acid binding
C	0038023	molecular_function	signaling receptor activity
C	0042803	molecular_function	protein homodimerization activity
D	0004864	molecular_function	protein phosphatase inhibitor activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0009738	biological_process	abscisic acid-activated signaling pathway
D	0010427	molecular_function	abscisic acid binding
D	0038023	molecular_function	signaling receptor activity
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	CYS146
A	HIS148
A	CYS208
A	CYS210

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	GLU172
A	GLU175
A	HOH530
D	GLU15

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 403

Chain	Residue
A	ASP327
A	ASP380
A	MG404
A	HOH502
A	HOH503
A	HOH590
A	ASP142

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 404

Chain	Residue
A	ASP142
A	GLY143
A	MG403
A	HOH501
A	HOH503
A	HOH524
A	HOH589

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 405

Chain	Residue
A	ASP327
A	ASP331
A	HOH561
A	HOH569

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	CYS146
B	HIS148
B	CYS208
B	CYS210

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	ASP142
B	ASP327
B	ASP380
B	MG403
B	HOH502
B	HOH503

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 403

Chain	Residue
B	ASP142
B	GLY143
B	MG402
B	HOH501
B	HOH503
B	HOH595
B	HOH596

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 404

Chain	Residue
B	GLU175
C	GLU15

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 405

Chain	Residue
B	ASP327
B	ASP331
B	HOH515
B	HOH572

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 201

Chain	Residue
B	HOH509
C	ASP74
C	HOH353
C	HOH354
C	HOH355

---

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG D 201

Chain	Residue
D	ASP74

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE137-GLY145

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O49686

Chain	Residue	Details
C	ALA73
B	CYS146
B	HIS148
B	CYS208
B	CYS210
B	ASP327
B	ASP331
B	ASP380
C	ARG100
C	GLU125
D	ALA73
D	ARG100
D	GLU125
A	ASP331
A	ASP380
B	ASP142

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686

Chain	Residue	Details
C	PRO72
C	SER136
D	PRO72
D	SER136

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7

Chain	Residue	Details
C	VAL144
D	VAL144

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