1SO2
CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 3B In COMPLEX WITH A DIHYDROPYRIDAZINE INHIBITOR
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
A | 0007165 | biological_process | signal transduction |
A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
B | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
B | 0007165 | biological_process | signal transduction |
B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
C | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
C | 0007165 | biological_process | signal transduction |
C | 0008081 | molecular_function | phosphoric diester hydrolase activity |
D | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
D | 0007165 | biological_process | signal transduction |
D | 0008081 | molecular_function | phosphoric diester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 471 |
Chain | Residue |
A | HOH11 |
A | HIS741 |
A | HIS821 |
A | ASP822 |
A | ASP937 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 472 |
Chain | Residue |
A | HOH15 |
A | ASP822 |
A | HOH11 |
A | HOH12 |
A | HOH13 |
A | HOH14 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 473 |
Chain | Residue |
B | HOH21 |
B | MG474 |
B | HIS741 |
B | HIS821 |
B | ASP822 |
B | ASP937 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 474 |
Chain | Residue |
B | HOH21 |
B | HOH22 |
B | HOH23 |
B | HOH24 |
B | HOH26 |
B | MG473 |
B | ASP822 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 475 |
Chain | Residue |
C | HOH31 |
C | HIS741 |
C | HIS821 |
C | ASP822 |
C | ASP937 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 476 |
Chain | Residue |
C | HOH31 |
C | HOH32 |
C | HOH33 |
C | HOH34 |
C | HOH36 |
C | ASP822 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 477 |
Chain | Residue |
D | HOH41 |
D | MG478 |
D | HIS741 |
D | HIS821 |
D | ASP822 |
D | ASP937 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MG D 478 |
Chain | Residue |
D | HOH41 |
D | HOH42 |
D | HOH43 |
D | HOH44 |
D | HOH46 |
D | MG477 |
D | HIS821 |
D | ASP822 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 479 |
Chain | Residue |
A | HOH51 |
A | HOH52 |
A | HOH53 |
A | HOH54 |
A | ASN968 |
B | ASP875 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HG9 B 451 |
Chain | Residue |
B | HOH223 |
B | HOH256 |
B | HOH385 |
B | HOH391 |
B | ASN957 |
B | ARG979 |
B | LEU984 |
D | ALA985 |
D | ILE1071 |
D | LYS1073 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HG9 B 452 |
Chain | Residue |
B | ALA985 |
B | LYS1070 |
B | ILE1071 |
B | LYS1073 |
D | LEU949 |
D | ASN957 |
D | TYR960 |
D | ARG979 |
D | LEU984 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HG9 A 453 |
Chain | Residue |
A | HOH126 |
A | HOH301 |
A | GLU953 |
A | ASN957 |
A | ARG979 |
A | LEU984 |
B | ARG783 |
C | ALA985 |
C | ILE1071 |
C | LYS1073 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HG9 A 454 |
Chain | Residue |
A | ALA985 |
A | ILE1071 |
A | LYS1073 |
C | HOH288 |
C | ASN957 |
C | ARG979 |
site_id | BC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 666 A 461 |
Chain | Residue |
A | THR952 |
A | LEU987 |
A | GLN988 |
A | SER990 |
A | PHE991 |
A | HOH148 |
A | HOH200 |
A | TYR736 |
A | THR829 |
A | ILE938 |
A | GLY940 |
A | PRO941 |
A | HIS948 |
A | TRP951 |
site_id | BC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 666 B 462 |
Chain | Residue |
B | TYR736 |
B | ILE938 |
B | GLY940 |
B | PRO941 |
B | HIS948 |
B | TRP951 |
B | THR952 |
B | PHE976 |
B | LEU987 |
B | GLN988 |
B | SER990 |
B | PHE991 |
site_id | BC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 666 C 463 |
Chain | Residue |
C | HOH182 |
C | TYR736 |
C | THR829 |
C | LEU895 |
C | ILE938 |
C | GLY940 |
C | PRO941 |
C | HIS948 |
C | THR952 |
C | LEU987 |
C | GLN988 |
C | SER990 |
C | PHE991 |
site_id | BC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 666 D 464 |
Chain | Residue |
D | HOH320 |
D | TYR736 |
D | THR829 |
D | ILE938 |
D | GLY940 |
D | PRO941 |
D | HIS948 |
D | TRP951 |
D | THR952 |
D | LEU987 |
D | GLN988 |
D | PHE991 |
Functional Information from PROSITE/UniProt
site_id | PS00126 |
Number of Residues | 12 |
Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDYdHpGrtNaF |
Chain | Residue | Details |
A | HIS821-PHE832 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083 |
Chain | Residue | Details |
A | HIS737 | |
B | HIS737 | |
C | HIS737 | |
D | HIS737 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q14432 |
Chain | Residue | Details |
A | HIS737 | |
A | GLN988 | |
B | HIS737 | |
B | GLN988 | |
C | HIS737 | |
C | GLN988 | |
D | HIS737 | |
D | GLN988 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15147193, ECO:0007744|PDB:1SO2, ECO:0007744|PDB:1SOJ |
Chain | Residue | Details |
A | HIS741 | |
D | HIS741 | |
D | HIS821 | |
D | ASP937 | |
A | HIS821 | |
A | ASP937 | |
B | HIS741 | |
B | HIS821 | |
B | ASP937 | |
C | HIS741 | |
C | HIS821 | |
C | ASP937 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15147193, ECO:0007744|PDB:1SO2 |
Chain | Residue | Details |
A | ASP822 | |
B | ASP822 | |
C | ASP822 | |
D | ASP822 |