2YPH

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H230S, crystallized with 2',3-(RP)- cyclic-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	5
Details	BINDING SITE FOR RESIDUE ACT A 1379

Chain	Residue
A	LYS223
A	ARG224
A	PRO225
A	CYS314
A	HOH2079

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1380

Chain	Residue
A	LYS273

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE QQY A 1381

Chain	Residue
A	HIS309
A	THR311
A	PRO320
A	VAL321
A	TYR168
A	THR232
A	PHE235

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22393399

Chain	Residue	Details
A	GLN250

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:22393399

Chain	Residue	Details
A	ASP329

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	VAL252
A	LEU331

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	PHE169

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13233

Chain	Residue	Details
A	GLY227
A	GLY239
A	ARG358

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