6VEB
Precorrin-2-bound S128A S. typhimurium siroheme synthase
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 | 0016491 | molecular_function | oxidoreductase 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 | 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 | 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 | 21 |
| Details | binding site for residue SAH A 501 |
| Chain | Residue |
| A | PRO225 |
| A | CYS336 |
| A | TYR381 |
| A | MET382 |
| A | VAL408 |
| A | ASN410 |
| A | GLY411 |
| A | PRO436 |
| A | ALA437 |
| A | LEU438 |
| A | HOH626 |
| A | LEU250 |
| A | HOH643 |
| A | HOH662 |
| A | GLY301 |
| A | GLY302 |
| A | ASP303 |
| A | ILE306 |
| A | PHE307 |
| A | THR331 |
| A | ALA332 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue NAD A 502 |
| Chain | Residue |
| A | GLY19 |
| A | GLY20 |
| A | GLY21 |
| A | ASP22 |
| A | VAL23 |
| A | ASN41 |
| A | ALA42 |
| A | LEU43 |
| A | THR44 |
| A | THR80 |
| A | ASP81 |
| A | VAL85 |
| A | HOH614 |
| A | HOH621 |
| A | HOH633 |
| B | ALA53 |
| B | ASN54 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | THR345 |
| A | HIS346 |
| A | ARG347 |
| A | ASP348 |
| A | TYR349 |
| A | ALA350 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | THR345 |
| B | PHE307 |
| B | ARG309 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| A | ALA128 |
| A | GLY130 |
| A | SER132 |
| A | PRO133 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | PHE307 |
| A | ARG309 |
| A | HOH668 |
| B | THR345 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue SAH B 501 |
| 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 | HOH634 |
| B | HOH655 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | LYS375 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | MET382 |
| B | LEU384 |
| site_id | AD1 |
| Number of Residues | 30 |
| Details | binding site for Di-peptide PQ2 B 502 and GLY B 130 |
| Chain | Residue |
| B | PRO133 |
| B | VAL134 |
| B | ARG137 |
| B | ARG140 |
| B | HOH603 |
| B | HOH609 |
| B | HOH643 |
| B | HOH683 |
| A | ARG162 |
| A | LYS166 |
| A | MET172 |
| A | ARG175 |
| A | ARG176 |
| A | TRP179 |
| A | ARG260 |
| A | ARG261 |
| A | ASP262 |
| B | LYS27 |
| B | ASN101 |
| B | VAL103 |
| B | ASP104 |
| B | PRO106 |
| B | ILE112 |
| B | MET113 |
| B | PRO114 |
| B | SER115 |
| B | ALA128 |
| B | GLY129 |
| B | THR131 |
| B | SER132 |
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 | PRO225 | |
| A | GLY301 | |
| A | ILE306 | |
| A | THR331 | |
| A | MET382 | |
| A | GLY411 | |
| A | ALA437 | |
| B | ASP22 | |
| B | LEU43 | |
| B | PRO225 | |
| B | GLY301 | |
| B | ILE306 | |
| B | THR331 | |
| B | MET382 | |
| B | GLY411 | |
| B | ALA437 | |
| A | ASP22 | |
| A | LEU43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:14595395 |
| Chain | Residue | Details |
| A | ALA128 | |
| B | ALA128 |
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 |
