4DJF
Crystal structure of folate-bound corrinoid iron-sulfur protein (CFeSP) in complex with its methyltransferase (MeTr), co-crystallized with folate and Ti(III) citrate reductant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008705 | molecular_function | methionine synthase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0032259 | biological_process | methylation |
| A | 0042558 | biological_process | pteridine-containing compound metabolic process |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050667 | biological_process | homocysteine metabolic process |
| A | 0071267 | biological_process | L-methionine salvage |
| A | 0102036 | molecular_function | methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008705 | molecular_function | methionine synthase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0032259 | biological_process | methylation |
| B | 0042558 | biological_process | pteridine-containing compound metabolic process |
| B | 0046653 | biological_process | tetrahydrofolate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050667 | biological_process | homocysteine metabolic process |
| B | 0071267 | biological_process | L-methionine salvage |
| B | 0102036 | molecular_function | methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0015977 | biological_process | carbon fixation |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0046356 | biological_process | acetyl-CoA catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0015977 | biological_process | carbon fixation |
| D | 0031419 | molecular_function | cobalamin binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0008168 | molecular_function | methyltransferase activity |
| E | 0015977 | biological_process | carbon fixation |
| E | 0031419 | molecular_function | cobalamin binding |
| E | 0046356 | biological_process | acetyl-CoA catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0006730 | biological_process | one-carbon metabolic process |
| F | 0015977 | biological_process | carbon fixation |
| F | 0031419 | molecular_function | cobalamin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C2F A 300 |
| Chain | Residue |
| A | GLU6 |
| A | GLN202 |
| A | ARG207 |
| A | MET11 |
| A | PHE12 |
| A | ASP75 |
| A | ASN96 |
| A | ILE120 |
| A | ASP160 |
| A | SER198 |
| A | ASN199 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 301 |
| Chain | Residue |
| A | GLY222 |
| A | ASP224 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE C2F B 300 |
| Chain | Residue |
| B | GLU6 |
| B | MET11 |
| B | PHE12 |
| B | ASP75 |
| B | ASN96 |
| B | LEU122 |
| B | ASP160 |
| B | GLY196 |
| B | SER198 |
| B | ASN199 |
| B | GLN202 |
| B | ARG207 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA B 301 |
| Chain | Residue |
| B | ASP224 |
| B | HOH402 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 C 501 |
| Chain | Residue |
| C | ASN16 |
| C | CYS17 |
| C | GLY18 |
| C | GLU19 |
| C | CYS20 |
| C | CYS25 |
| C | PHE28 |
| C | CYS42 |
| C | TYR44 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE COB C 502 |
| Chain | Residue |
| B | VAL168 |
| B | ASN199 |
| B | GLN202 |
| B | ASN203 |
| C | PRO318 |
| C | TYR338 |
| C | VAL339 |
| C | THR340 |
| C | THR346 |
| C | GLY370 |
| C | LEU371 |
| C | SER372 |
| C | VAL373 |
| C | THR375 |
| C | ALA378 |
| C | ASP379 |
| C | ILE406 |
| C | PRO408 |
| C | PRO430 |
| C | ARG431 |
| C | ALA433 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 E 501 |
| Chain | Residue |
| E | PRO13 |
| E | LYS15 |
| E | ASN16 |
| E | CYS17 |
| E | GLY18 |
| E | CYS20 |
| E | CYS25 |
| E | CYS42 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE COB E 502 |
| Chain | Residue |
| A | VAL168 |
| A | GLN202 |
| A | ASN203 |
| E | TYR338 |
| E | VAL339 |
| E | THR340 |
| E | PHE343 |
| E | THR346 |
| E | VAL350 |
| E | GLY370 |
| E | LEU371 |
| E | SER372 |
| E | VAL373 |
| E | LEU374 |
| E | THR375 |
| E | ALA378 |
| E | ASP379 |
| E | ILE406 |
| E | PRO408 |
| E | PRO430 |
| E | ARG431 |
| E | ALA433 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 490 |
| Details | Domain: {"description":"Pterin-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00334","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17172470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DJE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DJF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17172470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4DJF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17172470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DJF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 114 |
| Details | Domain: {"description":"4Fe-4S","evidences":[{"source":"PROSITE-ProRule","id":"PRU00989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DJD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22419154","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4DJD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






