3GWT
Catalytic domain of human phosphodiesterase 4B2B in complex with a quinoline inhibitor
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 066 A 1 |
Chain | Residue |
A | ARS4 |
A | PHE414 |
A | MET431 |
A | SER442 |
A | GLN443 |
A | PHE446 |
A | GOL508 |
A | HOH524 |
A | HOH527 |
A | HOH5 |
A | HOH56 |
A | TYR233 |
A | SER282 |
A | MET347 |
A | ASP392 |
A | ASN395 |
A | ILE410 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 504 |
Chain | Residue |
A | HOH74 |
A | HIS238 |
A | HIS274 |
A | ASP275 |
A | ASP392 |
A | HOH523 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 505 |
Chain | Residue |
A | HOH72 |
A | HOH73 |
A | HOH74 |
A | HOH75 |
A | HOH78 |
A | ASP275 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ARS A 506 |
Chain | Residue |
A | CYS194 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ARS A 2 |
Chain | Residue |
A | CYS320 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ARS A 3 |
Chain | Residue |
A | SER429 |
A | CYS432 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ARS A 4 |
Chain | Residue |
A | 0661 |
A | HIS234 |
A | HOH522 |
A | HOH523 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 507 |
Chain | Residue |
A | HOH10 |
A | HOH36 |
A | HOH115 |
A | ASP277 |
A | LEU293 |
A | HOH554 |
A | HOH649 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 508 |
Chain | Residue |
A | 0661 |
A | SER442 |
A | PHE446 |
A | HOH668 |
A | HOH683 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 509 |
Chain | Residue |
A | THR208 |
A | PHE209 |
A | ARG210 |
A | ASN325 |
A | GLN330 |
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 | HIS274-PHE285 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | HIS234 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 |
Chain | Residue | Details |
A | HIS234 | |
A | GLN443 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
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 | HIS238 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
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 | HIS274 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | ASP275 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
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 | ASP392 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 |
Chain | Residue | Details |
A | PHE446 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14646 |
Chain | Residue | Details |
A | ALA487 | |
A | ALA489 |