Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6CYB

PDE2 in complex with compound 7

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 1001
ChainResidue
AHIS660
AHIS696
AASP697
AASP808
AHOH1101
AHOH1202

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 1002
ChainResidue
AHOH1120
AHOH1137
AHOH1220
AASP697
AHOH1101
AHOH1103

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 1003
ChainResidue
ALEU770
APHE830
APHE862
AEDO1004
AFKV1008
AHOH1138

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 1004
ChainResidue
AASN704
APHE830
AEDO1003
AEDO1005
AHOH1110
AHOH1196

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 1005
ChainResidue
AASP769
ALEU770
AEDO1004
AHOH1157

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 1006
ChainResidue
AILE735
AASN739
ATYR754
AHOH1124
BARG751

site_idAC7
Number of Residues11
Detailsbinding site for residue EDO A 1007
ChainResidue
AARG608
ATYR655
AHIS660
ASER663
AVAL664
ACYS807
AASP808
ALEU809
ASER810
AASP811
AFKV1008

site_idAC8
Number of Residues18
Detailsbinding site for residue FKV A 1008
ChainResidue
ATYR655
AHIS656
ATHR768
ALEU770
ATHR805
AASP808
ALEU809
AASP811
AGLN812
AILE822
AILE826
AMET847
AGLN859
APHE862
AEDO1003
AEDO1007
AHOH1116
AHOH1197

site_idAC9
Number of Residues6
Detailsbinding site for residue ZN B 1001
ChainResidue
BHIS660
BHIS696
BASP697
BASP808
BHOH1101
BHOH1192

site_idAD1
Number of Residues6
Detailsbinding site for residue MG B 1002
ChainResidue
BASP697
BHOH1101
BHOH1104
BHOH1114
BHOH1157
BHOH1246

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 1003
ChainResidue
BPHE862
BILE866
BEDO1004
BFKV1006
BHOH1166

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO B 1004
ChainResidue
BASN704
BPHE830
BMET848
BEDO1003
BEDO1005
BHOH1207

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO B 1005
ChainResidue
BLEU770
BEDO1004
BHOH1103
BHOH1234

site_idAD5
Number of Residues17
Detailsbinding site for residue FKV B 1006
ChainResidue
BILE826
BGLN859
BPHE862
BEDO1003
BHOH1102
BHOH1119
BHOH1210
BTYR655
BHIS656
BTHR768
BLEU770
BTHR805
BASP808
BLEU809
BASP811
BGLN812
BILE822

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
ASER912
BSER912

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q922S4
ChainResidueDetails
APHE687
BGLN755
AGLY702
ASER721
AASN744
AGLN755
BPHE687
BGLY702
BSER721
BASN744

site_idSWS_FT_FI3
Number of Residues2
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

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon