1PJS
The co-crystal structure of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis, in complex with it NAD cofactor
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 | 0008152 | biological_process | metabolic 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 | 0008152 | biological_process | metabolic 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 | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 507 |
| Chain | Residue |
| A | ARG260 |
| A | ARG261 |
| A | HOH521 |
| A | HOH524 |
| B | SER115 |
| B | ARG137 |
| B | ARG140 |
| B | HOH513 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 501 |
| Chain | Residue |
| A | LEU250 |
| A | GLY301 |
| A | GLY302 |
| A | ASP303 |
| A | ILE306 |
| A | PHE307 |
| A | THR331 |
| A | ALA332 |
| A | CYS336 |
| A | TYR381 |
| A | MET382 |
| A | VAL408 |
| A | ASN410 |
| A | GLY411 |
| A | PRO436 |
| A | ALA437 |
| A | HOH576 |
| A | PRO225 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD A 502 |
| Chain | Residue |
| A | GLY19 |
| A | GLY20 |
| A | GLY21 |
| A | ASP22 |
| A | VAL23 |
| A | ALA42 |
| A | LEU43 |
| A | THR44 |
| A | GLY63 |
| A | THR80 |
| A | ASP81 |
| A | VAL85 |
| A | HOH591 |
| A | HOH595 |
| A | HOH604 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH B 503 |
| Chain | Residue |
| B | PRO225 |
| 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 | HOH526 |
| B | HOH576 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD B 504 |
| Chain | Residue |
| A | ASP264 |
| B | GLY20 |
| B | GLY21 |
| B | ASP22 |
| B | VAL23 |
| B | ARG26 |
| B | LEU43 |
| B | THR44 |
| B | THR80 |
| B | ASP81 |
| B | VAL85 |
| B | ASP104 |
| B | GLU281 |
| B | ARG288 |
| B | LYS292 |
| B | HOH558 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 505 |
| Chain | Residue |
| A | LEU139 |
| A | LYS142 |
| A | HOH513 |
| A | HOH577 |
| B | GLN241 |
| B | HOH616 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 506 |
| Chain | Residue |
| A | LEU146 |
| A | LEU151 |
| B | LEU139 |
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 | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:14595395 |
| Chain | Residue | Details |
| A | ASP248 | |
| B | ASP248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:14595395 |
| Chain | Residue | Details |
| A | LYS270 | |
| B | LYS270 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14595395 |
| Chain | Residue | Details |
| A | ASP22 | |
| B | ASP22 | |
| B | LEU43 | |
| B | PRO225 | |
| B | GLY301 | |
| B | ILE306 | |
| B | THR331 | |
| B | MET382 | |
| B | GLY411 | |
| B | ALA437 | |
| A | LEU43 | |
| A | PRO225 | |
| A | GLY301 | |
| A | ILE306 | |
| A | THR331 | |
| A | MET382 | |
| A | GLY411 | |
| A | ALA437 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:14595395 |
| Chain | Residue | Details |
| A | SEP128 | |
| B | SEP128 |
Catalytic Information from CSA
| 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 |
