4M3P
Betaine-Homocysteine S-Methyltransferase from Homo sapiens complexed with Homocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006577 | biological_process | amino-acid betaine metabolic process |
| A | 0006579 | biological_process | amino-acid betaine catabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008172 | molecular_function | S-methyltransferase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| A | 0047150 | molecular_function | betaine-homocysteine S-methyltransferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| A | 0071267 | biological_process | L-methionine salvage |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006577 | biological_process | amino-acid betaine metabolic process |
| B | 0006579 | biological_process | amino-acid betaine catabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008172 | molecular_function | S-methyltransferase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| B | 0047150 | molecular_function | betaine-homocysteine S-methyltransferase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| B | 0071267 | biological_process | L-methionine salvage |
| C | 0005634 | cellular_component | nucleus |
| C | 0005829 | cellular_component | cytosol |
| C | 0006577 | biological_process | amino-acid betaine metabolic process |
| C | 0006579 | biological_process | amino-acid betaine catabolic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008172 | molecular_function | S-methyltransferase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| C | 0047150 | molecular_function | betaine-homocysteine S-methyltransferase activity |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| C | 0071267 | biological_process | L-methionine salvage |
| D | 0005634 | cellular_component | nucleus |
| D | 0005829 | cellular_component | cytosol |
| D | 0006577 | biological_process | amino-acid betaine metabolic process |
| D | 0006579 | biological_process | amino-acid betaine catabolic process |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008172 | molecular_function | S-methyltransferase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| D | 0047150 | molecular_function | betaine-homocysteine S-methyltransferase activity |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| D | 0071267 | biological_process | L-methionine salvage |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | CYS217 |
| A | CYS299 |
| A | CYS300 |
| A | HCS703 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 702 |
| Chain | Residue |
| A | HOH825 |
| A | HOH945 |
| A | ASP26 |
| A | GLY27 |
| A | GLN72 |
| A | GLN247 |
| A | GLY298 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCS A 703 |
| Chain | Residue |
| A | GLY27 |
| A | PHE29 |
| A | VAL30 |
| A | GLN72 |
| A | GLU159 |
| A | TYR160 |
| A | CYS299 |
| A | ZN701 |
| A | HOH808 |
| A | HOH825 |
| A | HOH928 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SRT B 501 |
| Chain | Residue |
| A | GLU54 |
| A | ARG57 |
| B | ARG57 |
| B | ARG61 |
| B | HOH617 |
| B | HOH626 |
| B | HOH717 |
| C | LYS150 |
| C | LYS151 |
| C | ASN152 |
| C | HOH626 |
| C | HOH780 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | CYS217 |
| B | CYS299 |
| B | CYS300 |
| B | HCS504 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B 503 |
| Chain | Residue |
| B | ASP26 |
| B | GLY27 |
| B | GLN72 |
| B | GLN247 |
| B | GLY298 |
| B | HOH701 |
| B | HOH737 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCS B 504 |
| Chain | Residue |
| B | GLY27 |
| B | GLY28 |
| B | PHE29 |
| B | VAL30 |
| B | GLN72 |
| B | GLU159 |
| B | TYR160 |
| B | CYS299 |
| B | ZN502 |
| B | HOH642 |
| B | HOH701 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | CYS217 |
| C | CYS299 |
| C | CYS300 |
| C | HCS503 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K C 502 |
| Chain | Residue |
| C | ASP26 |
| C | GLY27 |
| C | GLN72 |
| C | GLN247 |
| C | GLY298 |
| C | HOH634 |
| C | HOH658 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCS C 503 |
| Chain | Residue |
| C | GLY27 |
| C | GLY28 |
| C | PHE29 |
| C | VAL30 |
| C | GLN72 |
| C | GLU159 |
| C | CYS299 |
| C | ZN501 |
| C | HOH628 |
| C | HOH658 |
| C | HOH759 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SRT D 501 |
| Chain | Residue |
| A | LYS150 |
| A | LYS151 |
| A | ASN152 |
| A | HOH822 |
| A | HOH877 |
| A | HOH881 |
| D | ARG57 |
| D | ARG61 |
| D | HOH611 |
| D | HOH625 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 502 |
| Chain | Residue |
| D | CYS217 |
| D | CYS299 |
| D | CYS300 |
| D | HCS504 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 503 |
| Chain | Residue |
| D | ASP26 |
| D | GLY27 |
| D | GLN72 |
| D | GLN247 |
| D | GLY298 |
| D | HOH684 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCS D 504 |
| Chain | Residue |
| D | GLY28 |
| D | PHE29 |
| D | VAL30 |
| D | GLN72 |
| D | GLU159 |
| D | TYR160 |
| D | CYS299 |
| D | ZN502 |
| D | HOH622 |
| D | HOH684 |
| D | GLY27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00333","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12220488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LT8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O35490","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O09171","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






