4DJD
Crystal structure of folate-free corrinoid iron-sulfur protein (CFeSP) in complex with its methyltransferase (MeTr)
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 301 |
| Chain | Residue |
| A | GLY222 |
| A | ASP224 |
| A | HOH427 |
| A | HOH430 |
| A | HOH433 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 301 |
| Chain | Residue |
| B | GLY222 |
| B | ASP224 |
| B | HOH422 |
| B | HOH430 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 C 501 |
| Chain | Residue |
| C | PRO13 |
| C | ASN16 |
| C | CYS17 |
| C | GLY18 |
| C | CYS20 |
| C | CYS25 |
| C | PHE28 |
| C | CYS42 |
| C | PRO43 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE B12 C 502 |
| Chain | Residue |
| B | VAL168 |
| C | PRO318 |
| C | VAL339 |
| C | THR340 |
| C | PHE343 |
| C | LEU345 |
| C | THR346 |
| C | VAL350 |
| C | GLY370 |
| C | LEU371 |
| C | SER372 |
| C | VAL373 |
| C | LEU374 |
| C | THR375 |
| C | ALA378 |
| C | ASP379 |
| C | GLY429 |
| C | PRO430 |
| C | ARG431 |
| C | GLU432 |
| C | ALA433 |
| D | PRO188 |
| D | LEU189 |
| D | TYR226 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 401 |
| Chain | Residue |
| D | ASP38 |
| D | PRO42 |
| D | PHE43 |
| D | ILE50 |
| D | PRO54 |
| D | ARG235 |
| D | LEU292 |
| D | GLY295 |
| D | ALA296 |
| D | HIS297 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 402 |
| Chain | Residue |
| D | ASP115 |
| D | HOH562 |
| F | GLY94 |
| F | ALA95 |
| F | ASP96 |
| F | LYS311 |
| F | HOH583 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 403 |
| Chain | Residue |
| D | ASP115 |
| F | ARG53 |
| F | ASP96 |
| F | LYS311 |
| F | ASP315 |
| F | HOH559 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 404 |
| Chain | Residue |
| D | HIS45 |
| D | ILE50 |
| D | HOH507 |
| E | GLU199 |
| E | ASN200 |
| E | HOH663 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 405 |
| Chain | Residue |
| D | LYS122 |
| D | GLN126 |
| D | GLU157 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 E 501 |
| Chain | Residue |
| E | PRO13 |
| E | LYS15 |
| E | ASN16 |
| E | CYS17 |
| E | GLY18 |
| E | GLU19 |
| E | CYS20 |
| E | CYS25 |
| E | CYS42 |
| site_id | BC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE B12 E 502 |
| Chain | Residue |
| E | ASP379 |
| E | PRO408 |
| E | PRO430 |
| E | ARG431 |
| E | GLU432 |
| E | ALA433 |
| F | PRO188 |
| F | LEU189 |
| F | TYR226 |
| A | VAL168 |
| A | ASN203 |
| E | PRO318 |
| E | TYR338 |
| E | VAL339 |
| E | THR340 |
| E | PHE343 |
| E | THR346 |
| E | SER349 |
| E | GLY370 |
| E | LEU371 |
| E | SER372 |
| E | VAL373 |
| E | LEU374 |
| E | THR375 |
| E | ALA378 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 503 |
| Chain | Residue |
| D | LYS170 |
| E | GLY210 |
| E | LEU211 |
| E | ASP244 |
| E | HOH614 |
| E | HOH655 |
| F | TYR323 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL E 504 |
| Chain | Residue |
| D | HIS144 |
| D | SER171 |
| D | HOH581 |
| E | ARG240 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL F 401 |
| Chain | Residue |
| F | ASP38 |
| F | PRO42 |
| F | PHE43 |
| F | ILE50 |
| F | PRO54 |
| F | ARG235 |
| F | LEU292 |
| F | GLY295 |
| F | ALA296 |
| F | HIS297 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 402 |
| Chain | Residue |
| D | GLU148 |
| D | ALA175 |
| D | HIS179 |
| F | HIS45 |
| F | ILE50 |
| F | MET318 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL F 403 |
| Chain | Residue |
| F | ASP8 |
| F | ARG9 |
| F | SER10 |
| F | GLN240 |
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 |






