3UJK

Crystal structure of protein phosphatase ABI2

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 424

Chain	Residue
A	HOH21
A	HOH40
A	ASP165
A	ASP337
A	ASP402

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 425

Chain	Residue
A	ASP337
A	HOH9
A	ASP165
A	ASP251
A	MET301

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 426

Chain	Residue
A	HOH12
A	HOH23
A	HOH24
A	HOH40
A	ASP165
A	GLY166

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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
A	PHE160-GLY168

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20729862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22116026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20729862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22116026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Site: {"description":"Lock","evidences":[{"source":"UniProtKB","id":"Q9CAJ0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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