1MKD
crystal structure of PDE4D catalytic domain and zardaverine complex
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 |
| E | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| E | 0007165 | biological_process | signal transduction |
| E | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| F | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| F | 0007165 | biological_process | signal transduction |
| F | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| G | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| G | 0007165 | biological_process | signal transduction |
| G | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| H | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| H | 0007165 | biological_process | signal transduction |
| H | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| I | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| I | 0007165 | biological_process | signal transduction |
| I | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| J | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| J | 0007165 | biological_process | signal transduction |
| J | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| K | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| K | 0007165 | biological_process | signal transduction |
| K | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| L | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| L | 0007165 | biological_process | signal transduction |
| L | 0008081 | molecular_function | phosphoric diester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 2001 |
| Chain | Residue |
| A | HIS261 |
| A | HIS297 |
| A | ASP298 |
| A | ASP415 |
| A | HOH1001 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 2002 |
| Chain | Residue |
| A | ASP298 |
| A | GLU327 |
| A | THR368 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2003 |
| Chain | Residue |
| B | HIS297 |
| B | ASP298 |
| B | ASP415 |
| B | MG2004 |
| B | HIS261 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 2004 |
| Chain | Residue |
| B | ASP298 |
| B | ZN2003 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 2005 |
| Chain | Residue |
| C | HIS261 |
| C | HIS297 |
| C | ASP298 |
| C | ASP415 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 2006 |
| Chain | Residue |
| C | ASP298 |
| C | GLU327 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 2007 |
| Chain | Residue |
| D | HIS261 |
| D | HIS297 |
| D | ASP298 |
| D | ASP415 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 2008 |
| Chain | Residue |
| D | ASP298 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 2009 |
| Chain | Residue |
| E | HIS261 |
| E | HIS297 |
| E | ASP298 |
| E | ASP415 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 2010 |
| Chain | Residue |
| E | HIS297 |
| E | ASP298 |
| E | GLU327 |
| E | THR368 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 2011 |
| Chain | Residue |
| F | HIS261 |
| F | HIS297 |
| F | ASP298 |
| F | ASP415 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG F 2012 |
| Chain | Residue |
| F | ASP298 |
| F | GLU327 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN G 2013 |
| Chain | Residue |
| G | HIS261 |
| G | HIS297 |
| G | ASP298 |
| G | ASP415 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG G 2014 |
| Chain | Residue |
| G | ASP298 |
| G | GLU327 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 2015 |
| Chain | Residue |
| H | HIS261 |
| H | HIS297 |
| H | ASP298 |
| H | ASP415 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG H 2016 |
| Chain | Residue |
| H | ASP298 |
| H | GLU327 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 2017 |
| Chain | Residue |
| I | HIS261 |
| I | HIS297 |
| I | ASP298 |
| I | ASP415 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG I 2018 |
| Chain | Residue |
| I | ASP298 |
| I | GLU327 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN J 2019 |
| Chain | Residue |
| J | HIS261 |
| J | HIS297 |
| J | ASP298 |
| J | ASP415 |
| J | MG2020 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG J 2020 |
| Chain | Residue |
| J | ASP298 |
| J | ZN2019 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN K 2021 |
| Chain | Residue |
| K | HIS261 |
| K | HIS297 |
| K | ASP298 |
| K | ASP415 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG K 2022 |
| Chain | Residue |
| K | HIS297 |
| K | ASP298 |
| K | THR368 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN L 2023 |
| Chain | Residue |
| L | HIS261 |
| L | HIS297 |
| L | ASP298 |
| L | ASP415 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG L 2024 |
| Chain | Residue |
| L | ASP298 |
| L | GLU327 |
| site_id | CC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR A 3001 |
| Chain | Residue |
| A | MET370 |
| A | ASN418 |
| A | PRO419 |
| A | TYR426 |
| A | TRP429 |
| A | THR430 |
| A | ILE433 |
| A | MET454 |
| A | GLN466 |
| A | PHE469 |
| site_id | CC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR B 3002 |
| Chain | Residue |
| B | MET370 |
| B | ASN418 |
| B | PRO419 |
| B | TYR426 |
| B | TRP429 |
| B | THR430 |
| B | ILE433 |
| B | MET454 |
| B | GLN466 |
| B | PHE469 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR C 3003 |
| Chain | Residue |
| C | ASN418 |
| C | PRO419 |
| C | TYR426 |
| C | TRP429 |
| C | THR430 |
| C | ILE433 |
| C | MET454 |
| C | GLN466 |
| C | PHE469 |
| C | MET370 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR D 3004 |
| Chain | Residue |
| D | MET370 |
| D | ASN418 |
| D | PRO419 |
| D | TYR426 |
| D | TRP429 |
| D | THR430 |
| D | ILE433 |
| D | MET454 |
| D | GLN466 |
| D | PHE469 |
| site_id | DC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR E 3005 |
| Chain | Residue |
| E | MET370 |
| E | ASN418 |
| E | PRO419 |
| E | TYR426 |
| E | TRP429 |
| E | THR430 |
| E | ILE433 |
| E | MET454 |
| E | GLN466 |
| E | PHE469 |
| site_id | DC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR F 3006 |
| Chain | Residue |
| F | MET370 |
| F | ASN418 |
| F | PRO419 |
| F | TYR426 |
| F | TRP429 |
| F | THR430 |
| F | ILE433 |
| F | MET454 |
| F | GLN466 |
| F | PHE469 |
| site_id | DC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ZAR G 3007 |
| Chain | Residue |
| G | MET370 |
| G | ASN418 |
| G | PRO419 |
| G | TYR426 |
| G | TRP429 |
| G | THR430 |
| G | ILE433 |
| G | MET454 |
| G | GLN466 |
| G | PHE469 |
| G | HOH1007 |
| site_id | DC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR H 3008 |
| Chain | Residue |
| H | MET370 |
| H | ASN418 |
| H | PRO419 |
| H | TYR426 |
| H | TRP429 |
| H | THR430 |
| H | ILE433 |
| H | MET454 |
| H | GLN466 |
| H | PHE469 |
| site_id | DC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ZAR I 3009 |
| Chain | Residue |
| I | MET370 |
| I | ASN418 |
| I | TYR426 |
| I | TRP429 |
| I | THR430 |
| I | ILE433 |
| I | MET454 |
| I | GLN466 |
| I | PHE469 |
| site_id | DC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR J 3010 |
| Chain | Residue |
| J | MET370 |
| J | ASN418 |
| J | PRO419 |
| J | TYR426 |
| J | TRP429 |
| J | THR430 |
| J | ILE433 |
| J | MET454 |
| J | GLN466 |
| J | PHE469 |
| site_id | DC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ZAR K 3011 |
| Chain | Residue |
| K | MET370 |
| K | ASN418 |
| K | TYR426 |
| K | TRP429 |
| K | THR430 |
| K | ILE433 |
| K | MET454 |
| K | GLN466 |
| K | PHE469 |
| site_id | DC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ZAR L 3012 |
| Chain | Residue |
| L | MET370 |
| L | ASN418 |
| L | PRO419 |
| L | TYR426 |
| L | TRP429 |
| L | THR430 |
| L | ILE433 |
| L | MET454 |
| L | GLN466 |
| L | PHE469 |
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 | HIS297-PHE308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343 |
| Chain | Residue | Details |
| A | HIS257 | |
| J | HIS257 | |
| K | HIS257 | |
| L | HIS257 | |
| B | HIS257 | |
| C | HIS257 | |
| D | HIS257 | |
| E | HIS257 | |
| F | HIS257 | |
| G | HIS257 | |
| H | HIS257 | |
| I | HIS257 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 |
| Chain | Residue | Details |
| A | HIS257 | |
| D | HIS257 | |
| D | ASN418 | |
| D | GLN466 | |
| E | HIS257 | |
| E | ASN418 | |
| E | GLN466 | |
| F | HIS257 | |
| F | ASN418 | |
| F | GLN466 | |
| G | HIS257 | |
| A | ASN418 | |
| G | ASN418 | |
| G | GLN466 | |
| H | HIS257 | |
| H | ASN418 | |
| H | GLN466 | |
| I | HIS257 | |
| I | ASN418 | |
| I | GLN466 | |
| J | HIS257 | |
| J | ASN418 | |
| A | GLN466 | |
| J | GLN466 | |
| K | HIS257 | |
| K | ASN418 | |
| K | GLN466 | |
| L | HIS257 | |
| L | ASN418 | |
| L | GLN466 | |
| B | HIS257 | |
| B | ASN418 | |
| B | GLN466 | |
| C | HIS257 | |
| C | ASN418 | |
| C | GLN466 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| 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 | HIS261 | |
| J | HIS261 | |
| K | HIS261 | |
| L | HIS261 | |
| B | HIS261 | |
| C | HIS261 | |
| D | HIS261 | |
| E | HIS261 | |
| F | HIS261 | |
| G | HIS261 | |
| H | HIS261 | |
| I | HIS261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| 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 | HIS297 | |
| E | ASP415 | |
| F | HIS297 | |
| F | ASP415 | |
| G | HIS297 | |
| G | ASP415 | |
| H | HIS297 | |
| H | ASP415 | |
| I | HIS297 | |
| I | ASP415 | |
| J | HIS297 | |
| A | ASP415 | |
| J | ASP415 | |
| K | HIS297 | |
| K | ASP415 | |
| L | HIS297 | |
| L | ASP415 | |
| B | HIS297 | |
| B | ASP415 | |
| C | HIS297 | |
| C | ASP415 | |
| D | HIS297 | |
| D | ASP415 | |
| E | HIS297 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
| Chain | Residue | Details |
| A | ASP298 | |
| E | PHE469 | |
| F | ASP298 | |
| F | PHE469 | |
| G | ASP298 | |
| G | PHE469 | |
| H | ASP298 | |
| H | PHE469 | |
| I | ASP298 | |
| I | PHE469 | |
| J | ASP298 | |
| A | PHE469 | |
| J | PHE469 | |
| K | ASP298 | |
| K | PHE469 | |
| L | ASP298 | |
| L | PHE469 | |
| B | ASP298 | |
| B | PHE469 | |
| C | ASP298 | |
| C | PHE469 | |
| D | ASP298 | |
| D | PHE469 | |
| E | ASP298 |
