4JA7

Rat PP5 co-crystallized with P5SA-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001965	molecular_function	G-protein alpha-subunit binding
A	0003723	molecular_function	RNA binding
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004722	molecular_function	protein serine/threonine phosphatase 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	0008017	molecular_function	microtubule binding
A	0010288	biological_process	response to lead ion
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
A	0030544	molecular_function	Hsp70 protein binding
A	0031072	molecular_function	heat shock protein binding
A	0031435	molecular_function	mitogen-activated protein kinase kinase kinase binding
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0043025	cellular_component	neuronal cell body
A	0043066	biological_process	negative regulation of apoptotic process
A	0043204	cellular_component	perikaryon
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0043278	biological_process	response to morphine
A	0043409	biological_process	negative regulation of MAPK cascade
A	0043531	molecular_function	ADP binding
A	0044877	molecular_function	protein-containing complex binding
A	0046872	molecular_function	metal ion binding
A	0051879	molecular_function	Hsp90 protein binding
A	0070262	biological_process	peptidyl-serine dephosphorylation
A	0070301	biological_process	cellular response to hydrogen peroxide
A	0071276	biological_process	cellular response to cadmium ion
A	0101031	cellular_component	protein folding chaperone complex
A	1904550	biological_process	response to arachidonate
A	1990635	cellular_component	proximal dendrite
A	2000324	biological_process	positive regulation of nuclear receptor-mediated glucocorticoid signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASP271
A	ASN303
A	HIS352
A	HIS427
A	MG502
A	HOH700

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	MG501
A	HOH610
A	ASP242
A	HIS244
A	ASP271

---

Functional Information from PROSITE/UniProt

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
A	LEU300-GLU305

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	33
Details	Repeat: {"description":"TPR 1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	33
Details	Repeat: {"description":"TPR 2"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	33
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P53041","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26182372","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JA7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P53041","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26182372","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JA7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JA9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---