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5U00

CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX WITH 3,3-difluoro-1-[(4-fluoro-3-iodophenyl)carbonyl]-5-{5-methyl-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl}piperidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
B0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
B0007165biological_processsignal transduction
B0008081molecular_functionphosphoric diester hydrolase activity
C0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
C0007165biological_processsignal transduction
C0008081molecular_functionphosphoric diester hydrolase activity
D0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
D0007165biological_processsignal transduction
D0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 7OV A 1001
ChainResidue
ATYR655
AHOH1296
DHIS587
AHIS656
ALEU770
AGLN812
ATYR827
APHE830
AMET847
AGLN859
APHE862

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 1002
ChainResidue
AHIS660
AHIS696
AASP697
AASP808
AHOH1195
AHOH1230

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 1003
ChainResidue
AASP697
AHOH1136
AHOH1173
AHOH1195
AHOH1211
AHOH1228

site_idAC4
Number of Residues10
Detailsbinding site for residue 7OV B 1001
ChainResidue
BTYR655
BHIS656
BLEU770
BGLN812
BTYR827
BPHE830
BMET847
BGLN859
BPHE862
BHOH1277

site_idAC5
Number of Residues6
Detailsbinding site for residue ZN B 1002
ChainResidue
BHIS660
BHIS696
BASP697
BASP808
BHOH1130
BHOH1251

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 1003
ChainResidue
BASP697
BHOH1130
BHOH1155
BHOH1162
BHOH1174
BHOH1234

site_idAC7
Number of Residues12
Detailsbinding site for residue 7OV C 1001
ChainResidue
CTYR655
CHIS656
CLEU770
CGLN812
CILE826
CTYR827
CPHE830
CMET847
CGLN859
CPHE862
CHOH1219
CHOH1303

site_idAC8
Number of Residues6
Detailsbinding site for residue ZN C 1002
ChainResidue
CHIS660
CHIS696
CASP697
CASP808
CHOH1132
CHOH1219

site_idAC9
Number of Residues6
Detailsbinding site for residue MG C 1003
ChainResidue
CASP697
CHOH1130
CHOH1132
CHOH1178
CHOH1200
CHOH1237

site_idAD1
Number of Residues11
Detailsbinding site for residue 7OV D 1001
ChainResidue
DTYR655
DHIS656
DLEU770
DGLN812
DILE826
DTYR827
DPHE830
DMET847
DGLN859
DPHE862
DHOH1268

site_idAD2
Number of Residues6
Detailsbinding site for residue ZN D 1002
ChainResidue
DHIS660
DHIS696
DASP697
DASP808
DHOH1131
DHOH1209

site_idAD3
Number of Residues6
Detailsbinding site for residue MG D 1003
ChainResidue
DASP697
DHOH1131
DHOH1147
DHOH1175
DHOH1208
DHOH1240

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGtnNsF
ChainResidueDetails
AHIS696-PHE707

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
ASER912
BSER912
CSER912
DSER912

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q922S4
ChainResidueDetails
AGLN755
BPHE687
BGLY702
BSER721
BASN744
BGLN755
CPHE687
CGLY702
CSER721
CASN744
CGLN755
DPHE687
DGLY702
DSER721
DASN744
DGLN755
APHE687
AGLY702
ASER721
AASN744

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287, ECO:0007744|PDB:1Z1L, ECO:0007744|PDB:3IBJ, ECO:0007744|PDB:3ITM, ECO:0007744|PDB:3ITU, ECO:0007744|PDB:4HTX, ECO:0007744|PDB:4HTZ, ECO:0007744|PDB:4JIB
ChainResidueDetails
ALEU916
BLEU916
CLEU916
DLEU916

221051

PDB entries from 2024-06-12

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