5OHJ
Human phosphodiesterase 4B catalytic domain in complex with a pyrrolidinyl 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue ZN A 699 |
Chain | Residue |
A | HIS410 |
A | HIS446 |
A | ASP447 |
A | ASP564 |
A | HOH714 |
A | HOH745 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 700 |
Chain | Residue |
A | HOH747 |
A | HOH748 |
A | HOH749 |
A | ASP447 |
A | HOH745 |
A | HOH746 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue 9VE A 801 |
Chain | Residue |
A | SER454 |
A | THR517 |
A | MET519 |
A | ASP564 |
A | LEU565 |
A | ASN567 |
A | PRO568 |
A | TYR575 |
A | TRP578 |
A | THR579 |
A | ILE582 |
A | PHE586 |
A | GLN589 |
A | PRO602 |
A | MET603 |
A | CYS604 |
A | SER614 |
A | GLN615 |
A | PHE618 |
A | ILE622 |
A | HOH751 |
A | HOH784 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ZN B 699 |
Chain | Residue |
B | HIS410 |
B | HIS446 |
B | ASP447 |
B | ASP564 |
B | HOH702 |
B | HOH752 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 700 |
Chain | Residue |
B | ASP447 |
B | HOH741 |
B | HOH744 |
B | HOH747 |
B | HOH748 |
B | HOH752 |
site_id | AC6 |
Number of Residues | 20 |
Details | binding site for residue 9VE B 801 |
Chain | Residue |
B | SER454 |
B | THR517 |
B | MET519 |
B | ASP564 |
B | LEU565 |
B | ASN567 |
B | PRO568 |
B | TYR575 |
B | TRP578 |
B | THR579 |
B | ILE582 |
B | PHE586 |
B | GLN589 |
B | PRO602 |
B | MET603 |
B | SER614 |
B | GLN615 |
B | PHE618 |
B | ILE622 |
B | HOH750 |
Functional Information from PROSITE/UniProt
site_id | PS00126 |
Number of Residues | 12 |
Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF |
Chain | Residue | Details |
A | HIS446-PHE457 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | ALA411 | |
B | ALA411 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 |
Chain | Residue | Details |
A | ALA411 | |
A | ASP620 | |
B | ALA411 | |
B | ASP620 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P |
Chain | Residue | Details |
A | ALA415 | |
B | ALA415 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P |
Chain | Residue | Details |
A | PRO451 | |
B | PRO451 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | GLY452 | |
B | GLY452 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:3D3P |
Chain | Residue | Details |
A | THR569 | |
B | THR569 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 |
Chain | Residue | Details |
A | VAL623 | |
B | VAL623 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14646 |
Chain | Residue | Details |
A | LYS295 | |
A | HIS664 | |
B | LYS295 | |
B | HIS664 |