1KYW
Crystal Structure Analysis of Caffeic Acid/5-hydroxyferulic acid 3/5-O-methyltransferase in complex with 5-hydroxyconiferaldehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0009699 | biological_process | phenylpropanoid biosynthetic process |
| A | 0009809 | biological_process | lignin biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0047763 | molecular_function | caffeate O-methyltransferase activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0009699 | biological_process | phenylpropanoid biosynthetic process |
| C | 0009809 | biological_process | lignin biosynthetic process |
| C | 0032259 | biological_process | methylation |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 0047763 | molecular_function | caffeate O-methyltransferase activity |
| F | 0008168 | molecular_function | methyltransferase activity |
| F | 0008171 | molecular_function | O-methyltransferase activity |
| F | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| F | 0009699 | biological_process | phenylpropanoid biosynthetic process |
| F | 0009809 | biological_process | lignin biosynthetic process |
| F | 0032259 | biological_process | methylation |
| F | 0046983 | molecular_function | protein dimerization activity |
| F | 0047763 | molecular_function | caffeate O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SAH C 1698 |
| Chain | Residue |
| C | GLY208 |
| C | HOH1713 |
| C | ASP231 |
| C | LEU232 |
| C | ASP251 |
| C | MET252 |
| C | PHE253 |
| C | LYS265 |
| C | TRP266 |
| C | TRP271 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH F 1699 |
| Chain | Residue |
| F | SER184 |
| F | GLY208 |
| F | ASP231 |
| F | LEU232 |
| F | GLY250 |
| F | ASP251 |
| F | MET252 |
| F | PHE253 |
| F | LYS265 |
| F | TRP266 |
| F | TRP271 |
| F | HOH1743 |
| F | HOH1766 |
| F | HOH1767 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HFL F 0 |
| Chain | Residue |
| F | LEU136 |
| F | ALA162 |
| F | MET180 |
| F | ASP270 |
| F | MET320 |
| F | HIS323 |
| F | ASN324 |
| F | HOH1714 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000305|PubMed:12084826 |
| Chain | Residue | Details |
| A | HIS269 | |
| C | HIS269 | |
| F | HIS269 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:F1DBB3 |
| Chain | Residue | Details |
| A | GLU297 | |
| A | GLU329 | |
| C | GLU297 | |
| C | GLU329 | |
| F | GLU297 | |
| F | GLU329 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12084826, ECO:0007744|PDB:1KYZ |
| Chain | Residue | Details |
| A | ASN131 | |
| C | ASP231 | |
| C | ASP251 | |
| C | MET252 | |
| C | MET264 | |
| C | LYS265 | |
| F | ASN131 | |
| F | GLY208 | |
| F | ASP231 | |
| F | ASP251 | |
| F | MET252 | |
| A | GLY208 | |
| F | MET264 | |
| F | LYS265 | |
| A | ASP231 | |
| A | ASP251 | |
| A | MET252 | |
| A | MET264 | |
| A | LYS265 | |
| C | ASN131 | |
| C | GLY208 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12084826, ECO:0007744|PDB:1KYW |
| Chain | Residue | Details |
| A | ASP270 | |
| C | ASP270 | |
| F | ASP270 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12084826, 11224575 |
| Chain | Residue | Details |
| A | HIS269 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12084826, 11224575 |
| Chain | Residue | Details |
| C | HIS269 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12084826, 11224575 |
| Chain | Residue | Details |
| F | HIS269 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 621 |
| Chain | Residue | Details |
| A | HIS269 | proton acceptor, proton donor |
| A | ASP270 | electrostatic stabiliser, steric role |
| A | GLU297 | electrostatic stabiliser, steric role |
| A | GLU329 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 621 |
| Chain | Residue | Details |
| C | HIS269 | proton acceptor, proton donor |
| C | ASP270 | electrostatic stabiliser, steric role |
| C | GLU297 | electrostatic stabiliser, steric role |
| C | GLU329 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 621 |
| Chain | Residue | Details |
| F | HIS269 | proton acceptor, proton donor |
| F | ASP270 | electrostatic stabiliser, steric role |
| F | GLU297 | electrostatic stabiliser, steric role |
| F | GLU329 | electrostatic stabiliser, hydrogen bond donor, steric role |
