3G4G
Crystal structure of human phosphodiesterase 4d with regulatory domain and d155871
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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 801 |
Chain | Residue |
A | HOH50 |
A | HIS330 |
A | HIS366 |
A | ASP367 |
A | ASP484 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 802 |
Chain | Residue |
A | HOH80 |
A | ASP367 |
A | HOH586 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA A 4 |
Chain | Residue |
A | HIS271 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE D71 A 901 |
Chain | Residue |
A | HOH54 |
A | HOH154 |
A | PHE196 |
A | ILE197 |
A | PHE201 |
A | TYR325 |
A | HIS326 |
A | LEU485 |
A | ASN487 |
A | THR499 |
A | ILE502 |
A | MET503 |
A | PHE506 |
A | SER534 |
A | GLN535 |
A | PHE538 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 803 |
Chain | Residue |
B | HOH59 |
B | HIS330 |
B | HIS366 |
B | ASP367 |
B | ASP484 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 804 |
Chain | Residue |
B | HOH96 |
B | HOH118 |
B | ASP367 |
B | HOH586 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE D71 B 902 |
Chain | Residue |
B | HOH82 |
B | VAL193 |
B | PHE196 |
B | ILE197 |
B | TYR325 |
B | HIS326 |
B | LEU485 |
B | ASN487 |
B | THR499 |
B | ILE502 |
B | PHE506 |
B | SER534 |
B | GLN535 |
B | PHE538 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 805 |
Chain | Residue |
C | HOH34 |
C | HIS330 |
C | HIS366 |
C | ASP367 |
C | ASP484 |
C | HOH587 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 806 |
Chain | Residue |
C | HOH72 |
C | HOH88 |
C | ASP367 |
C | HOH587 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA C 2 |
Chain | Residue |
C | HIS271 |
C | ARG274 |
site_id | BC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE D71 C 903 |
Chain | Residue |
C | HOH31 |
C | PHE196 |
C | ILE197 |
C | TYR325 |
C | HIS326 |
C | LEU485 |
C | ASN487 |
C | THR499 |
C | ILE502 |
C | PHE506 |
C | MET523 |
C | SER534 |
C | GLN535 |
C | PHE538 |
C | HOH586 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 807 |
Chain | Residue |
D | HOH21 |
D | HIS330 |
D | HIS366 |
D | ASP367 |
D | ASP484 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 808 |
Chain | Residue |
D | HOH6 |
D | HOH67 |
D | HOH84 |
D | HOH140 |
D | ASP367 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA D 3 |
Chain | Residue |
D | HIS271 |
site_id | BC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE D71 D 904 |
Chain | Residue |
D | HOH33 |
D | VAL193 |
D | PHE196 |
D | ILE197 |
D | TYR325 |
D | HIS326 |
D | LEU485 |
D | ASN487 |
D | THR499 |
D | ILE502 |
D | SER534 |
D | GLN535 |
D | PHE538 |
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 | HIS366-PHE377 |
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 | HIS326 | |
B | HIS326 | |
C | HIS326 | |
D | HIS326 |
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 | HIS326 | |
D | HIS326 | |
D | ASN487 | |
D | GLN535 | |
A | ASN487 | |
A | GLN535 | |
B | HIS326 | |
B | ASN487 | |
B | GLN535 | |
C | HIS326 | |
C | ASN487 | |
C | GLN535 |
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 | HIS330 | |
B | HIS330 | |
C | HIS330 | |
D | HIS330 |
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 | HIS366 | |
A | ASP484 | |
B | HIS366 | |
B | ASP484 | |
C | HIS366 | |
C | ASP484 | |
D | HIS366 | |
D | ASP484 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
Chain | Residue | Details |
A | ASP367 | |
A | PHE538 | |
B | ASP367 | |
B | PHE538 | |
C | ASP367 | |
C | PHE538 | |
D | ASP367 | |
D | PHE538 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
A | SER163 | |
A | SER165 | |
B | SER163 | |
B | SER165 | |
C | SER163 | |
C | SER165 | |
D | SER163 | |
D | SER165 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER239 | |
B | SER239 | |
C | SER239 | |
D | SER239 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
Chain | Residue | Details |
A | LYS251 | |
B | LYS251 | |
C | LYS251 | |
D | LYS251 |