2YP0

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, crystallized with 2'-AMPS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004113	molecular_function	2',3'-cyclic-nucleotide 3'-phosphodiesterase activity
A	0009214	biological_process	cyclic nucleotide catabolic process
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue OVE A 401

Chain	Residue
A	TYR168
A	HOH560
A	HIS230
A	THR232
A	PHE235
A	HIS309
A	THR311
A	PRO320
A	VAL321
A	HOH526

---

site_id	AC2
Number of Residues	3
Details	binding site for residue GOL A 402

Chain	Residue
A	PHE169
A	ALA248
A	TYR257

---

site_id	AC3
Number of Residues	4
Details	binding site for residue OVE A 403

Chain	Residue
A	ARG203
A	HIS204
A	LYS356
A	HOH552

---

site_id	AC4
Number of Residues	6
Details	binding site for residue 1PE A 404

Chain	Residue
A	GLY258
A	LYS259
A	ALA260
A	PHE261
A	GLN284
A	ILE372

---

site_id	AC5
Number of Residues	7
Details	binding site for residue ACY A 405

Chain	Residue
A	TRP289
A	PRO303
A	PRO304
A	GLY305
A	SER306
A	ARG307
A	HOH559

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22393399","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22393399","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13233","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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