1PJT
The structure of the Ser128Ala point-mutant variant of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0004851 | molecular_function | uroporphyrin-III C-methyltransferase activity |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0019354 | biological_process | siroheme biosynthetic process |
| A | 0043115 | molecular_function | precorrin-2 dehydrogenase activity |
| A | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004325 | molecular_function | ferrochelatase activity |
| B | 0004851 | molecular_function | uroporphyrin-III C-methyltransferase activity |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0019354 | biological_process | siroheme biosynthetic process |
| B | 0043115 | molecular_function | precorrin-2 dehydrogenase activity |
| B | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 503 |
| Chain | Residue |
| A | ARG261 |
| A | ASP262 |
| A | HOH522 |
| B | SER115 |
| B | ARG137 |
| B | ARG140 |
| B | HOH535 |
| B | HOH552 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH A 501 |
| Chain | Residue |
| A | GLY301 |
| A | GLY302 |
| A | ASP303 |
| A | ILE306 |
| A | PHE307 |
| A | THR331 |
| A | ALA332 |
| A | TYR381 |
| A | MET382 |
| A | VAL408 |
| A | GLY411 |
| A | PRO436 |
| A | ALA437 |
| A | HOH543 |
| A | HOH581 |
| A | PRO225 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH B 502 |
| Chain | Residue |
| B | PRO225 |
| B | LEU250 |
| B | GLY301 |
| B | GLY302 |
| B | ASP303 |
| B | ILE306 |
| B | PHE307 |
| B | THR331 |
| B | ALA332 |
| B | CYS336 |
| B | TYR381 |
| B | MET382 |
| B | VAL408 |
| B | ASN410 |
| B | GLY411 |
| B | PRO436 |
| B | ALA437 |
| B | LEU438 |
| B | HOH538 |
| B | HOH539 |
Functional Information from PROSITE/UniProt
| site_id | PS00839 |
| Number of Residues | 15 |
| Details | SUMT_1 Uroporphyrin-III C-methyltransferase signature 1. VGAGPGdagLLTLKG |
| Chain | Residue | Details |
| A | VAL221-GLY235 |
| site_id | PS00840 |
| Number of Residues | 34 |
| Details | SUMT_2 Uroporphyrin-III C-methyltransferase signature 2. VvrLkgGDpfiFGrggeeletLchagipFsVvPG |
| Chain | Residue | Details |
| A | VAL296-GLY329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 396 |
| Details | Region: {"description":"Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelatase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kyq |
| Chain | Residue | Details |
| A | ASP104 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kyq |
| Chain | Residue | Details |
| B | ASP104 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 702 |
| Chain | Residue | Details |
| A | ASP248 | electrostatic stabiliser, proton acceptor, proton donor |
| A | LYS270 | electrostatic stabiliser |
| A | MET382 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 702 |
| Chain | Residue | Details |
| B | ASP248 | electrostatic stabiliser, proton acceptor, proton donor |
| B | LYS270 | electrostatic stabiliser |
| B | MET382 | electrostatic stabiliser |
