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4JIB

Crystal structure of of PDE2-inhibitor complex

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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS660
AHIS696
AASP697
AASP808
AHOH1120
AHOH1454

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
AHOH1445
AHOH1454
AHOH1465
AASP697
AHOH1216
AHOH1269

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1L6 A 1003
ChainResidue
ATYR655
ALEU809
AASP811
AGLN812
ATYR827
AMET847
ALEU858
AGLN859
ASER861
APHE862
AHOH1102
AHOH1110
AHOH1360
DHIS587
DHOH1228

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BHIS660
BHIS696
BASP697
BASP808
BHOH1103
BHOH1456

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BASP697
BHOH1284
BHOH1442
BHOH1450
BHOH1456
BHOH1457

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1L6 B 1003
ChainResidue
BTYR655
BLEU809
BGLN812
BTYR827
BMET847
BLEU858
BGLN859
BSER861
BPHE862
BHOH1102
BHOH1105

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 1001
ChainResidue
CHIS660
CHIS696
CASP697
CASP808
CHOH1107
CHOH1425

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 1002
ChainResidue
CASP697
CHOH1122
CHOH1410
CHOH1415
CHOH1424
CHOH1425

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1L6 C 1003
ChainResidue
BGLN591
CTYR655
CLEU770
CLEU809
CASP811
CGLN812
CILE826
CPHE830
CMET847
CPHE862
CHOH1102
CHOH1104
CHOH1127
CHOH1172

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN D 1001
ChainResidue
DHIS660
DHIS696
DASP697
DASP808
DHOH1120
DHOH1176

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1002
ChainResidue
DASP697
DHOH1176
DHOH1429
DHOH1436
DHOH1446
DHOH1459

site_idBC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 1L6 D 1003
ChainResidue
DHOH1113
DHOH1120
DHOH1252
DHOH1311
DHOH1458
AGLN591
DTYR655
DLEU770
DASP811
DGLN812
DILE826
DPHE830
DMET847
DSER861
DPHE862
DHOH1103

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
AHIS656
BHIS656
CHIS656
DHIS656

site_idSWS_FT_FI2
Number of Residues12
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
CASP808
DHIS660
DASP697
DASP808
AHIS660
AASP697
AASP808
BHIS660
BASP697
BASP808
CHIS660
CASP697

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:3ITM, ECO:0007744|PDB:3ITU, ECO:0007744|PDB:4HTX, ECO:0007744|PDB:4HTZ, ECO:0007744|PDB:4JIB
ChainResidueDetails
AHIS696
BHIS696
CHIS696
DHIS696

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PDB entries from 2024-06-12

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