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3ZBR

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H230S, crystallized with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004113molecular_function2',3'-cyclic-nucleotide 3'-phosphodiesterase activity
A0009214biological_processcyclic nucleotide catabolic process
A0016020cellular_componentmembrane
B0004113molecular_function2',3'-cyclic-nucleotide 3'-phosphodiesterase activity
B0009214biological_processcyclic nucleotide catabolic process
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAP A 1379
ChainResidue
ALEU167
AGLY378
AHOH2020
AHOH2021
AHOH2039
AHOH2051
ATYR168
ATHR232
APHE235
AHIS309
ATHR311
APRO320
AVAL321
ATYR376

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NAP B 1379
ChainResidue
BLEU167
BPRO226
BTHR232
BPHE235
BHIS309
BTHR311
BPRO320
BVAL321
BTYR376
BHOH2014
BHOH2031

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22393399","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22393399","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13233","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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