2V69
Crystal structure of Chlamydomonas reinhardtii Rubisco with a large- subunit mutation D473E
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009853 | biological_process | photorespiration |
| A | 0015977 | biological_process | carbon fixation |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009853 | biological_process | photorespiration |
| B | 0015977 | biological_process | carbon fixation |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0009507 | cellular_component | chloroplast |
| C | 0009853 | biological_process | photorespiration |
| C | 0015977 | biological_process | carbon fixation |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019253 | biological_process | reductive pentose-phosphate cycle |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0009507 | cellular_component | chloroplast |
| D | 0009853 | biological_process | photorespiration |
| D | 0015977 | biological_process | carbon fixation |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0019253 | biological_process | reductive pentose-phosphate cycle |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0009507 | cellular_component | chloroplast |
| E | 0009853 | biological_process | photorespiration |
| E | 0015977 | biological_process | carbon fixation |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0009507 | cellular_component | chloroplast |
| F | 0009853 | biological_process | photorespiration |
| F | 0015977 | biological_process | carbon fixation |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0019253 | biological_process | reductive pentose-phosphate cycle |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0009507 | cellular_component | chloroplast |
| G | 0009853 | biological_process | photorespiration |
| G | 0015977 | biological_process | carbon fixation |
| G | 0015979 | biological_process | photosynthesis |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| G | 0019253 | biological_process | reductive pentose-phosphate cycle |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0009507 | cellular_component | chloroplast |
| H | 0009853 | biological_process | photorespiration |
| H | 0015977 | biological_process | carbon fixation |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1470 |
| Chain | Residue |
| A | LYS177 |
| A | KCX201 |
| A | ASP203 |
| A | GLU204 |
| A | CAP1471 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP A1471 |
| Chain | Residue |
| A | ASP203 |
| A | GLU204 |
| A | HIS294 |
| A | ARG295 |
| A | HIS327 |
| A | LYS334 |
| A | LEU335 |
| A | SER379 |
| A | GLY380 |
| A | GLY381 |
| A | GLY403 |
| A | GLY404 |
| A | HOH1049 |
| A | HOH1050 |
| A | MG1470 |
| B | GLU60 |
| B | THR65 |
| B | TRP66 |
| B | ASN123 |
| A | THR173 |
| A | LYS175 |
| A | LYS177 |
| A | KCX201 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B1470 |
| Chain | Residue |
| B | LYS177 |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| B | CAP1471 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CAP B1471 |
| Chain | Residue |
| A | GLU60 |
| A | THR65 |
| A | TRP66 |
| A | ASN123 |
| B | THR173 |
| B | LYS175 |
| B | LYS177 |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| B | HIS294 |
| B | ARG295 |
| B | HIS327 |
| B | LYS334 |
| B | LEU335 |
| B | SER379 |
| B | GLY380 |
| B | GLY381 |
| B | GLY403 |
| B | GLY404 |
| B | HOH1029 |
| B | MG1470 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C1471 |
| Chain | Residue |
| C | LYS177 |
| C | KCX201 |
| C | ASP203 |
| C | GLU204 |
| C | CAP1472 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP C1472 |
| Chain | Residue |
| C | THR173 |
| C | LYS175 |
| C | LYS177 |
| C | KCX201 |
| C | ASP203 |
| C | GLU204 |
| C | HIS294 |
| C | ARG295 |
| C | HIS327 |
| C | LYS334 |
| C | LEU335 |
| C | SER379 |
| C | GLY380 |
| C | GLY381 |
| C | GLY403 |
| C | GLY404 |
| C | HOH1051 |
| C | HOH1056 |
| C | MG1471 |
| D | GLU60 |
| D | THR65 |
| D | TRP66 |
| D | ASN123 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D1475 |
| Chain | Residue |
| D | LYS177 |
| D | KCX201 |
| D | ASP203 |
| D | GLU204 |
| D | CAP1476 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP D1476 |
| Chain | Residue |
| D | HIS294 |
| D | ARG295 |
| D | HIS327 |
| D | LYS334 |
| D | LEU335 |
| D | SER379 |
| D | GLY380 |
| D | GLY381 |
| D | GLY403 |
| D | GLY404 |
| D | HOH1029 |
| D | HOH1035 |
| D | HOH1036 |
| D | MG1475 |
| C | GLU60 |
| C | THR65 |
| C | TRP66 |
| C | ASN123 |
| C | HOH1015 |
| D | THR173 |
| D | LYS175 |
| D | LYS177 |
| D | KCX201 |
| D | ASP203 |
| D | GLU204 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E1470 |
| Chain | Residue |
| E | LYS177 |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| E | CAP1471 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP E1471 |
| Chain | Residue |
| E | THR173 |
| E | LYS175 |
| E | LYS177 |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| E | HIS294 |
| E | ARG295 |
| E | HIS327 |
| E | LYS334 |
| E | LEU335 |
| E | SER379 |
| E | GLY380 |
| E | GLY381 |
| E | GLY403 |
| E | GLY404 |
| E | HOH1048 |
| E | HOH1049 |
| E | MG1470 |
| F | GLU60 |
| F | THR65 |
| F | TRP66 |
| F | ASN123 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F1470 |
| Chain | Residue |
| F | LYS177 |
| F | KCX201 |
| F | ASP203 |
| F | GLU204 |
| F | CAP1471 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP F1471 |
| Chain | Residue |
| E | GLU60 |
| E | THR65 |
| E | TRP66 |
| E | ASN123 |
| F | THR173 |
| F | LYS175 |
| F | LYS177 |
| F | KCX201 |
| F | ASP203 |
| F | GLU204 |
| F | HIS294 |
| F | ARG295 |
| F | HIS327 |
| F | LYS334 |
| F | LEU335 |
| F | SER379 |
| F | GLY380 |
| F | GLY381 |
| F | GLY403 |
| F | GLY404 |
| F | HOH1039 |
| F | HOH1040 |
| F | MG1470 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G1470 |
| Chain | Residue |
| G | LYS177 |
| G | KCX201 |
| G | ASP203 |
| G | GLU204 |
| G | CAP1471 |
| site_id | BC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP G1471 |
| Chain | Residue |
| G | THR173 |
| G | LYS175 |
| G | LYS177 |
| G | KCX201 |
| G | ASP203 |
| G | GLU204 |
| G | HIS294 |
| G | ARG295 |
| G | HIS327 |
| G | LYS334 |
| G | LEU335 |
| G | SER379 |
| G | GLY380 |
| G | GLY381 |
| G | GLY403 |
| G | GLY404 |
| G | HOH1035 |
| G | HOH1041 |
| G | MG1470 |
| H | GLU60 |
| H | THR65 |
| H | TRP66 |
| H | ASN123 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H1470 |
| Chain | Residue |
| H | LYS177 |
| H | KCX201 |
| H | ASP203 |
| H | GLU204 |
| H | CAP1471 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CAP H1471 |
| Chain | Residue |
| G | GLU60 |
| G | THR65 |
| G | TRP66 |
| G | ASN123 |
| H | THR173 |
| H | LYS175 |
| H | LYS177 |
| H | KCX201 |
| H | ASP203 |
| H | GLU204 |
| H | HIS294 |
| H | ARG295 |
| H | HIS327 |
| H | LYS334 |
| H | LEU335 |
| H | SER379 |
| H | GLY380 |
| H | GLY381 |
| H | GLY403 |
| H | GLY404 |
| H | HOH1040 |
| H | MG1470 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1472 |
| Chain | Residue |
| A | LYS18 |
| A | ASP19 |
| A | TRP66 |
| A | THR67 |
| A | THR68 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A1473 |
| Chain | Residue |
| A | LYS466 |
| A | PHE467 |
| A | GLU468 |
| A | PHE469 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C1473 |
| Chain | Residue |
| C | TYR24 |
| C | THR68 |
| C | VAL69 |
| C | ASP72 |
| C | HOH1057 |
| C | EDO1474 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C1474 |
| Chain | Residue |
| C | LYS18 |
| C | TYR20 |
| C | THR65 |
| C | TRP66 |
| C | THR67 |
| C | THR68 |
| C | HOH1057 |
| C | EDO1473 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C1475 |
| Chain | Residue |
| C | ARG295 |
| C | GLU336 |
| C | HOH1043 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E1472 |
| Chain | Residue |
| E | TYR24 |
| E | THR68 |
| E | VAL69 |
| E | ASP72 |
| E | HOH1053 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO E1473 |
| Chain | Residue |
| E | LYS18 |
| E | TYR20 |
| E | THR65 |
| E | TRP66 |
| E | THR67 |
| E | THR68 |
| E | HOH1002 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO E1474 |
| Chain | Residue |
| E | GLU52 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO G1472 |
| Chain | Residue |
| G | TYR24 |
| G | THR68 |
| G | VAL69 |
| G | ASP72 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO G1473 |
| Chain | Residue |
| G | LYS18 |
| G | ASP19 |
| G | TYR20 |
| G | THR65 |
| G | TRP66 |
| G | THR67 |
| G | THR68 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO E1475 |
| Chain | Residue |
| E | LEU270 |
| E | HOH1054 |
| F | LEU270 |
| F | HOH1028 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A1474 |
| Chain | Residue |
| A | LEU270 |
| A | HOH1051 |
| A | HOH1052 |
| B | LEU270 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO H1472 |
| Chain | Residue |
| G | LEU270 |
| H | LEU270 |
| H | HOH1041 |
| H | HOH1042 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1472 |
| Chain | Residue |
| B | TYR24 |
| B | GLY64 |
| B | THR68 |
| B | VAL69 |
| B | ASP72 |
| B | EDO1473 |
| site_id | DC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1473 |
| Chain | Residue |
| B | LYS18 |
| B | TYR20 |
| B | THR65 |
| B | TRP66 |
| B | THR67 |
| B | THR68 |
| B | EDO1472 |
| site_id | DC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO H1473 |
| Chain | Residue |
| H | TYR24 |
| H | GLY64 |
| H | THR68 |
| H | VAL69 |
| H | ASP72 |
| H | HOH1043 |
| H | EDO1474 |
| site_id | DC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO H1474 |
| Chain | Residue |
| H | LYS18 |
| H | ASP19 |
| H | TRP66 |
| H | THR67 |
| H | THR68 |
| H | EDO1473 |
| site_id | DC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO H1475 |
| Chain | Residue |
| H | LYS466 |
| H | PHE467 |
| H | GLU468 |
| site_id | DC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO F1472 |
| Chain | Residue |
| F | TYR24 |
| F | THR68 |
| F | VAL69 |
| F | ASP72 |
| F | LEU77 |
| F | HOH1041 |
| F | EDO1473 |
| site_id | DC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO F1473 |
| Chain | Residue |
| F | LYS18 |
| F | ASP19 |
| F | THR65 |
| F | TRP66 |
| F | THR67 |
| F | THR68 |
| F | EDO1472 |
| site_id | EC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D1477 |
| Chain | Residue |
| D | TYR24 |
| D | GLY64 |
| D | THR68 |
| D | VAL69 |
| D | ASP72 |
| D | HOH1002 |
| site_id | EC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D1478 |
| Chain | Residue |
| D | LYS18 |
| D | ASP19 |
| D | THR65 |
| D | TRP66 |
| D | THR67 |
| D | THR68 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D1479 |
| Chain | Residue |
| C | LEU270 |
| C | THR271 |
| D | LEU270 |
| D | GLY273 |
| D | PHE274 |
| site_id | EC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO G1474 |
| Chain | Residue |
| E | ASP286 |
| E | ASN287 |
| E | HOH1039 |
| G | ARG215 |
| G | LYS252 |
| G | SMC256 |
| M | VAL63 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE |
| Chain | Residue | Details |
| A | GLY196-GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | MOD_RES: N-methylmethionine => ECO:0000269|PubMed:11641402 |
| Chain | Residue | Details |
| I | MME1 | |
| J | MME1 | |
| K | MME1 | |
| L | MME1 | |
| M | MME1 | |
| N | MME1 | |
| O | MME1 | |
| P | MME1 | |
| E | LYS175 | |
| E | HIS294 | |
| F | LYS175 | |
| F | HIS294 | |
| G | LYS175 | |
| G | HIS294 | |
| H | LYS175 | |
| H | HIS294 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in homodimeric partner |
| Chain | Residue | Details |
| A | ASN123 | |
| B | ASN123 | |
| C | ASN123 | |
| D | ASN123 | |
| E | ASN123 | |
| F | ASN123 | |
| G | ASN123 | |
| H | ASN123 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: |
| Chain | Residue | Details |
| D | LYS177 | |
| D | ARG295 | |
| D | HIS327 | |
| D | SER379 | |
| E | THR173 | |
| E | LYS177 | |
| E | ARG295 | |
| E | HIS327 | |
| E | SER379 | |
| F | THR173 | |
| F | LYS177 | |
| F | ARG295 | |
| F | HIS327 | |
| F | SER379 | |
| G | THR173 | |
| G | LYS177 | |
| G | ARG295 | |
| G | HIS327 | |
| G | SER379 | |
| H | THR173 | |
| H | LYS177 | |
| H | ARG295 | |
| H | HIS327 | |
| H | SER379 | |
| A | THR173 | |
| A | LYS177 | |
| A | ARG295 | |
| A | HIS327 | |
| A | SER379 | |
| B | THR173 | |
| B | LYS177 | |
| B | ARG295 | |
| B | HIS327 | |
| B | SER379 | |
| C | THR173 | |
| C | LYS177 | |
| C | ARG295 | |
| C | HIS327 | |
| C | SER379 | |
| D | THR173 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526 |
| Chain | Residue | Details |
| A | KCX201 | |
| B | KCX201 | |
| C | KCX201 | |
| D | KCX201 | |
| E | KCX201 | |
| F | KCX201 | |
| G | KCX201 | |
| H | KCX201 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526 |
| Chain | Residue | Details |
| A | ASP203 | |
| A | GLU204 | |
| B | ASP203 | |
| B | GLU204 | |
| C | ASP203 | |
| C | GLU204 | |
| D | ASP203 | |
| D | GLU204 | |
| E | ASP203 | |
| E | GLU204 | |
| F | ASP203 | |
| F | GLU204 | |
| G | ASP203 | |
| G | GLU204 | |
| H | ASP203 | |
| H | GLU204 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS334 | |
| B | LYS334 | |
| C | LYS334 | |
| D | LYS334 | |
| E | LYS334 | |
| F | LYS334 | |
| G | LYS334 | |
| H | LYS334 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylproline => ECO:0000269|PubMed:16668742 |
| Chain | Residue | Details |
| A | PRO3 | |
| B | PRO3 | |
| C | PRO3 | |
| D | PRO3 | |
| E | PRO3 | |
| F | PRO3 | |
| G | PRO3 | |
| H | PRO3 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | MOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526 |
| Chain | Residue | Details |
| A | HYP104 | |
| A | HYP151 | |
| B | HYP104 | |
| B | HYP151 | |
| C | HYP104 | |
| C | HYP151 | |
| D | HYP104 | |
| D | HYP151 | |
| E | HYP104 | |
| E | HYP151 | |
| F | HYP104 | |
| F | HYP151 | |
| G | HYP104 | |
| G | HYP151 | |
| H | HYP104 | |
| H | HYP151 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526, ECO:0000269|PubMed:6302265 |
| Chain | Residue | Details |
| A | KCX201 | |
| B | KCX201 | |
| C | KCX201 | |
| D | KCX201 | |
| E | KCX201 | |
| F | KCX201 | |
| G | KCX201 | |
| H | KCX201 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | MOD_RES: S-methylcysteine => ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526 |
| Chain | Residue | Details |
| A | SMC256 | |
| A | SMC369 | |
| B | SMC256 | |
| B | SMC369 | |
| C | SMC256 | |
| C | SMC369 | |
| D | SMC256 | |
| D | SMC369 | |
| E | SMC256 | |
| E | SMC369 | |
| F | SMC256 | |
| F | SMC369 | |
| G | SMC256 | |
| G | SMC369 | |
| H | SMC256 | |
| H | SMC369 |
