4WDB

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation R307Q, complexed with 2'-AMP

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	13
Details	binding site for residue 2AM A 401

Chain	Residue
A	TYR168
A	GLY324
A	HOH551
A	HOH554
A	HOH577
A	HIS230
A	THR232
A	PHE235
A	HIS309
A	THR311
A	PRO320
A	VAL321
A	THR323

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CL A 402

Chain	Residue
A	TRP289
A	SER297
A	GLY305
A	GLN307
A	HOH531

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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

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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

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

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13233","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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