6C07
Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | GLY288 |
| A | ALA289 |
| A | LYS293 |
| B | ARG272 |
| B | HOH714 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | HOH786 |
| B | HOH643 |
| A | ASP266 |
| A | ALA267 |
| A | HOH682 |
| A | HOH692 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | ASP139 |
| A | HOH632 |
| A | HOH729 |
| A | HOH773 |
| A | HOH822 |
| B | HOH679 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | GLY182 |
| B | HOH647 |
| B | HOH694 |
| B | HOH766 |
| B | HOH795 |
| B | HOH811 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| A | HOH698 |
| B | ASP266 |
| B | ALA267 |
| B | HOH671 |
| B | HOH705 |
| B | HOH763 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue K C 501 |
| Chain | Residue |
| C | GLY271 |
| D | GLY271 |
| D | HOH709 |
| D | HOH776 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | HIS34 |
| C | LYS189 |
| C | LYS273 |
| C | HOH797 |
| C | HOH824 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 503 |
| Chain | Residue |
| C | ASP266 |
| C | ALA267 |
| C | HOH609 |
| C | HOH653 |
| C | HOH845 |
| D | HOH642 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 504 |
| Chain | Residue |
| C | ASP139 |
| C | HOH642 |
| C | HOH703 |
| C | HOH747 |
| C | HOH832 |
| D | HOH638 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 501 |
| Chain | Residue |
| D | ASP36 |
| D | LYS273 |
| D | HOH615 |
| D | HOH639 |
| D | HOH653 |
| D | HOH686 |
| D | HOH803 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 10 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGrFTIGGP |
| Chain | Residue | Details |
| A | PRO254-PRO263 |
| site_id | PS00376 |
| Number of Residues | 11 |
| Details | ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGmmfGY |
| Chain | Residue | Details |
| A | GLY136-TYR146 |
| site_id | PS00377 |
| Number of Residues | 9 |
| Details | ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD |
| Chain | Residue | Details |
| A | GLY286-ASP294 |
