3B5I
Crystal structure of Indole-3-acetic Acid Methyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009851 | biological_process | auxin biosynthetic process |
| A | 0009944 | biological_process | polarity specification of adaxial/abaxial axis |
| A | 0032259 | biological_process | methylation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051749 | molecular_function | indole acetic acid carboxyl methyltransferase activity |
| A | 0103007 | molecular_function | indole-3-acetate carboxyl methyltransferase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005575 | cellular_component | cellular_component |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009851 | biological_process | auxin biosynthetic process |
| B | 0009944 | biological_process | polarity specification of adaxial/abaxial axis |
| B | 0032259 | biological_process | methylation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051749 | molecular_function | indole acetic acid carboxyl methyltransferase activity |
| B | 0103007 | molecular_function | indole-3-acetate carboxyl methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH A 401 |
| Chain | Residue |
| A | GLY60 |
| A | ALA157 |
| A | PHE158 |
| A | SER159 |
| A | HOH603 |
| A | HOH607 |
| A | HOH609 |
| A | HOH613 |
| A | CYS61 |
| A | SER62 |
| A | ASN66 |
| A | ASP98 |
| A | LEU99 |
| A | SER140 |
| A | PHE141 |
| A | TYR142 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | ASN179 |
| A | VAL183 |
| A | ARG265 |
| A | ASP266 |
| A | PHE268 |
| A | ASN269 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH B 401 |
| Chain | Residue |
| B | GLY60 |
| B | CYS61 |
| B | ASN66 |
| B | ASP98 |
| B | LEU99 |
| B | GLY139 |
| B | SER140 |
| B | PHE141 |
| B | TYR142 |
| B | ALA157 |
| B | PHE158 |
| B | SER159 |
| B | HOH620 |
| B | HOH624 |
| B | HOH626 |
| B | HOH638 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | ASN179 |
| B | VAL183 |
| B | ARG265 |
| B | ASP266 |
| B | PHE268 |
| B | ASN269 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A4GE70 |
| Chain | Residue | Details |
| A | TYR18 | |
| A | PHE96 | |
| A | PHE158 | |
| B | TYR18 | |
| B | PHE96 | |
| B | PHE158 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A4GE69 |
| Chain | Residue | Details |
| A | ASN21 | |
| A | GLY60 | |
| A | SER322 | |
| B | ASN21 | |
| B | GLY60 | |
| B | SER322 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18162595, ECO:0007744|PDB:3B5I |
| Chain | Residue | Details |
| A | ASN66 | |
| A | ASN269 | |
| B | ASN66 | |
| B | ASP98 | |
| B | SER140 | |
| B | ALA157 | |
| B | ASN179 | |
| B | VAL183 | |
| B | ARG265 | |
| B | ASP266 | |
| B | PHE268 | |
| A | ASP98 | |
| B | ASN269 | |
| A | SER140 | |
| A | ALA157 | |
| A | ASN179 | |
| A | VAL183 | |
| A | ARG265 | |
| A | ASP266 | |
| A | PHE268 |
