6J23
Crystal structure of arabidopsis ADAL complexed with GMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004000 | molecular_function | adenosine deaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006154 | biological_process | adenosine catabolic process |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0046103 | biological_process | inosine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0062154 | molecular_function | N6-methyl-AMP deaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue 5GP A 401 |
| Chain | Residue |
| A | HIS15 |
| A | ASP160 |
| A | GLY190 |
| A | HIS217 |
| A | GLU220 |
| A | ASN295 |
| A | ASP296 |
| A | HOH507 |
| A | HOH520 |
| A | HOH528 |
| A | HOH544 |
| A | LEU16 |
| A | HOH586 |
| A | HOH614 |
| A | HOH637 |
| A | ASN17 |
| A | PHE58 |
| A | PHE61 |
| A | HIS65 |
| A | THR97 |
| A | THR98 |
| A | LYS100 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS13 |
| A | HIS15 |
| A | HIS217 |
| A | ASN295 |
| A | HOH507 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P03958 |
| Chain | Residue | Details |
| A | GLU220 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30721978, ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJM, ECO:0007744|PDB:6IV5 |
| Chain | Residue | Details |
| A | HIS13 | |
| A | HIS15 | |
| A | HIS217 | |
| A | ASN295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30721978, ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN, ECO:0007744|PDB:6J4T |
| Chain | Residue | Details |
| A | ASN17 | |
| A | HIS65 | |
| A | THR97 | |
| A | ASP160 | |
| A | GLY190 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30721978, ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJP, ECO:0007744|PDB:6J4T |
| Chain | Residue | Details |
| A | GLU220 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30721978, ECO:0007744|PDB:6IJP |
| Chain | Residue | Details |
| A | ASP296 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P03958 |
| Chain | Residue | Details |
| A | HIS240 |
