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2YOZ

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 Residues12
DetailsBINDING SITE FOR RESIDUE OVE A 1379
ChainResidue
ATYR168
AHOH2033
AHOH2071
AHOH2074
AHIS230
ATHR232
APHE235
AHIS309
ATHR311
APRO320
AVAL321
ATHR323

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1380
ChainResidue
AARG348
ALYS366

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE A 1381
ChainResidue
AALA197
ALYS200
ASER353

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 1382
ChainResidue
APHE198
ATHR271
APRO272
AGLY357

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 1383
ChainResidue
ALYS223
AARG224
APRO225
AHOH2073

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 1384
ChainResidue
ALYS262

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1385
ChainResidue
ATRP289
ASER297
AGLY305

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 1386
ChainResidue
ALYS370
AHOH2094

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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