1PJQ
Structure and function of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019354 | biological_process | siroheme biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0043115 | molecular_function | precorrin-2 dehydrogenase activity |
| A | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019354 | biological_process | siroheme biosynthetic process |
| B | 0032259 | biological_process | methylation |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 503 |
| Chain | Residue |
| B | MET113 |
| B | SER115 |
| B | SEP128 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 504 |
| Chain | Residue |
| A | HOH577 |
| A | GLY19 |
| A | GLY20 |
| A | THR44 |
| A | THR80 |
| A | ASP81 |
| A | HOH576 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 505 |
| Chain | Residue |
| A | GLY301 |
| A | GLY302 |
| A | ASP303 |
| A | ILE306 |
| A | PHE307 |
| A | THR331 |
| A | ALA332 |
| A | TYR381 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE A 502 |
| Chain | Residue |
| A | LEU139 |
| A | LYS142 |
| B | GLN241 |
| B | HOH567 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH B 501 |
| Chain | Residue |
| B | PRO225 |
| B | GLY301 |
| 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 | HOH541 |
| B | HOH543 |
| B | HOH650 |
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 | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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 |
| Chain | Residue | Details |
| A | ASP248 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 702 |
| Chain | Residue | Details |
| A | SER252 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLN386 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 702 |
| Chain | Residue | Details |
| B | SER252 | electrostatic stabiliser, proton acceptor, proton donor |
| B | GLN386 | electrostatic stabiliser |
