1XLX
Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Cilomilast
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 1001 |
Chain | Residue |
A | HIS238 |
A | HIS274 |
A | ASP275 |
A | ASP392 |
A | HOH1007 |
A | HOH1008 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 1002 |
Chain | Residue |
A | HOH1004 |
A | HOH1005 |
A | HOH1006 |
A | HOH1007 |
A | CIO101 |
A | ASP275 |
A | HOH1003 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 1001 |
Chain | Residue |
B | HIS238 |
B | HIS274 |
B | ASP275 |
B | ASP392 |
B | HOH2007 |
B | HOH2008 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1002 |
Chain | Residue |
B | ASP275 |
B | HOH2003 |
B | HOH2004 |
B | HOH2005 |
B | HOH2006 |
B | HOH2007 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CIO A 101 |
Chain | Residue |
A | HOH2 |
A | HOH60 |
A | HOH61 |
A | MET347 |
A | ASN395 |
A | ILE410 |
A | MET411 |
A | PHE414 |
A | SER442 |
A | GLN443 |
A | PHE446 |
A | MG1002 |
A | HOH1006 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIO B 102 |
Chain | Residue |
B | HOH22 |
B | HOH43 |
B | TYR233 |
B | MET347 |
B | ASN395 |
B | THR407 |
B | ILE410 |
B | MET411 |
B | SER442 |
B | GLN443 |
B | PHE446 |
B | HOH2006 |
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 | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | HIS234 | |
B | HIS234 |
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 | HIS234 | |
A | GLN443 | |
B | HIS234 | |
B | GLN443 |
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 | HIS238 | |
B | HIS238 |
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 | HIS274 | |
B | HIS274 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR |
Chain | Residue | Details |
A | ASP275 | |
B | ASP275 |
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 | ASP392 | |
B | ASP392 |
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 | PHE446 | |
B | PHE446 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14646 |
Chain | Residue | Details |
A | SER487 | |
A | SER489 | |
B | SER487 | |
B | SER489 |