2FM5
Crystal structure of PDE4D2 in complex with inhibitor L-869299
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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | HIS164 |
A | HIS200 |
A | ASP201 |
A | ASP318 |
A | HOH602 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | HOH605 |
A | HOH606 |
A | HOH607 |
A | ASP201 |
A | HOH603 |
A | HOH604 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 503 |
Chain | Residue |
B | HIS164 |
B | HIS200 |
B | ASP201 |
B | ASP318 |
B | HOH603 |
B | HOH608 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 504 |
Chain | Residue |
B | ASP201 |
B | HOH604 |
B | HOH605 |
B | HOH606 |
B | HOH607 |
B | HOH608 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 505 |
Chain | Residue |
C | HIS164 |
C | HIS200 |
C | ASP201 |
C | ASP318 |
C | HOH604 |
C | HOH609 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 506 |
Chain | Residue |
C | ASP201 |
C | HOH605 |
C | HOH606 |
C | HOH607 |
C | HOH608 |
C | HOH609 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN D 507 |
Chain | Residue |
D | HIS164 |
D | HIS200 |
D | ASP201 |
D | ASP318 |
D | HOH605 |
D | HOH610 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 508 |
Chain | Residue |
D | ASP201 |
D | HOH606 |
D | HOH607 |
D | HOH608 |
D | HOH609 |
D | HOH610 |
site_id | AC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE M99 A 601 |
Chain | Residue |
A | THR271 |
A | MET273 |
A | ASP318 |
A | ASN321 |
A | PRO322 |
A | TYR329 |
A | TRP332 |
A | THR333 |
A | ILE336 |
A | MET357 |
A | GLN369 |
A | PHE372 |
A | ILE376 |
A | HOH606 |
A | HOH614 |
A | HOH615 |
A | HOH637 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE M99 B 602 |
Chain | Residue |
B | THR271 |
B | MET273 |
B | ASP318 |
B | ASN321 |
B | PRO322 |
B | TYR329 |
B | TRP332 |
B | THR333 |
B | ILE336 |
B | MET357 |
B | GLN369 |
B | PHE372 |
B | ILE376 |
B | HOH615 |
B | HOH616 |
site_id | BC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE M99 C 603 |
Chain | Residue |
C | THR271 |
C | MET273 |
C | ASP318 |
C | ASN321 |
C | PRO322 |
C | TYR329 |
C | TRP332 |
C | THR333 |
C | ILE336 |
C | MET357 |
C | GLN369 |
C | PHE372 |
C | ILE376 |
C | HOH605 |
C | HOH608 |
C | HOH613 |
C | HOH615 |
C | HOH640 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE M99 D 604 |
Chain | Residue |
D | MET273 |
D | ASP318 |
D | ASN321 |
D | PRO322 |
D | TYR329 |
D | TRP332 |
D | THR333 |
D | ILE336 |
D | MET357 |
D | GLN369 |
D | PHE372 |
D | ILE376 |
D | HOH639 |
D | HOH675 |
D | THR271 |
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 | HIS200-PHE211 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343 |
Chain | Residue | Details |
A | HIS160 | |
B | HIS160 | |
C | HIS160 | |
D | HIS160 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 |
Chain | Residue | Details |
A | HIS160 | |
D | HIS160 | |
D | ASN321 | |
D | GLN369 | |
A | ASN321 | |
A | GLN369 | |
B | HIS160 | |
B | ASN321 | |
B | GLN369 | |
C | HIS160 | |
C | ASN321 | |
C | GLN369 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 |
Chain | Residue | Details |
A | HIS164 | |
B | HIS164 | |
C | HIS164 | |
D | HIS164 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 |
Chain | Residue | Details |
A | HIS200 | |
A | ASP318 | |
B | HIS200 | |
B | ASP318 | |
C | HIS200 | |
C | ASP318 | |
D | HIS200 | |
D | ASP318 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
Chain | Residue | Details |
A | ASP201 | |
A | PHE372 | |
B | ASP201 | |
B | PHE372 | |
C | ASP201 | |
C | PHE372 | |
D | ASP201 | |
D | PHE372 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
Chain | Residue | Details |
A | LYS85 | |
B | LYS85 | |
C | LYS85 | |
D | LYS85 |