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2YP0

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004113molecular_function2',3'-cyclic-nucleotide 3'-phosphodiesterase activity
A0009214biological_processcyclic nucleotide catabolic process
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue OVE A 401
ChainResidue
ATYR168
AHOH560
AHIS230
ATHR232
APHE235
AHIS309
ATHR311
APRO320
AVAL321
AHOH526

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 402
ChainResidue
APHE169
AALA248
ATYR257

site_idAC3
Number of Residues4
Detailsbinding site for residue OVE A 403
ChainResidue
AARG203
AHIS204
ALYS356
AHOH552

site_idAC4
Number of Residues6
Detailsbinding site for residue 1PE A 404
ChainResidue
AGLY258
ALYS259
AALA260
APHE261
AGLN284
AILE372

site_idAC5
Number of Residues7
Detailsbinding site for residue ACY A 405
ChainResidue
ATRP289
APRO303
APRO304
AGLY305
ASER306
AARG307
AHOH559

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:22393399
ChainResidueDetails
AGLN250

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:22393399
ChainResidueDetails
AASP329

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AVAL252
ALEU331

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
APHE169

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13233
ChainResidueDetails
AGLY227
AGLY239
AARG358

226707

PDB entries from 2024-10-30

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