1UWA
L290F mutant rubisco from chlamydomonas
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0009507 | cellular_component | chloroplast |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009507 | cellular_component | chloroplast |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0009507 | cellular_component | chloroplast |
| E | 0015977 | biological_process | carbon fixation |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0009507 | cellular_component | chloroplast |
| H | 0015977 | biological_process | carbon fixation |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0019253 | biological_process | reductive pentose-phosphate cycle |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0009507 | cellular_component | chloroplast |
| K | 0015977 | biological_process | carbon fixation |
| K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| K | 0019253 | biological_process | reductive pentose-phosphate cycle |
| O | 0000287 | molecular_function | magnesium ion binding |
| O | 0009507 | cellular_component | chloroplast |
| O | 0015977 | biological_process | carbon fixation |
| O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| O | 0019253 | biological_process | reductive pentose-phosphate cycle |
| R | 0000287 | molecular_function | magnesium ion binding |
| R | 0009507 | cellular_component | chloroplast |
| R | 0015977 | biological_process | carbon fixation |
| R | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| R | 0019253 | biological_process | reductive pentose-phosphate cycle |
| V | 0000287 | molecular_function | magnesium ion binding |
| V | 0009507 | cellular_component | chloroplast |
| V | 0015977 | biological_process | carbon fixation |
| V | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| V | 0019253 | biological_process | reductive pentose-phosphate cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 476 |
| Chain | Residue |
| A | KCX201 |
| A | ASP203 |
| A | GLU204 |
| A | CAP502 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 476 |
| Chain | Residue |
| B | LYS177 |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| B | CAP502 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 476 |
| Chain | Residue |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| E | CAP502 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG H 476 |
| Chain | Residue |
| H | KCX201 |
| H | ASP203 |
| H | GLU204 |
| H | CAP502 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG K 476 |
| Chain | Residue |
| K | KCX201 |
| K | ASP203 |
| K | GLU204 |
| K | CAP502 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG O 476 |
| Chain | Residue |
| O | KCX201 |
| O | ASP203 |
| O | GLU204 |
| O | CAP502 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG R 476 |
| Chain | Residue |
| R | LYS177 |
| R | KCX201 |
| R | ASP203 |
| R | GLU204 |
| R | CAP502 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG V 476 |
| Chain | Residue |
| V | KCX201 |
| V | ASP203 |
| V | GLU204 |
| V | CAP502 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP A 477 |
| Chain | Residue |
| A | THR173 |
| A | LYS175 |
| A | LYS177 |
| A | KCX201 |
| 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 | MG501 |
| A | HOH667 |
| A | HOH639 |
| A | HOH646 |
| A | HOH607 |
| A | HOH627 |
| A | HOH648 |
| O | GLU60 |
| O | THR65 |
| O | TRP66 |
| O | ASN123 |
| O | HOH676 |
| site_id | BC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP B 477 |
| Chain | Residue |
| 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 | MG501 |
| B | HOH689 |
| B | HOH713 |
| B | HOH627 |
| B | HOH609 |
| B | HOH633 |
| B | HOH640 |
| E | GLU60 |
| E | THR65 |
| E | TRP66 |
| E | ASN123 |
| E | HOH705 |
| E | HOH708 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 1 |
| Chain | Residue |
| A | HOH713 |
| A | TYR24 |
| A | GLY64 |
| A | THR68 |
| A | VAL69 |
| A | ASP72 |
| A | LEU77 |
| A | HOH677 |
| A | HOH654 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 2 |
| Chain | Residue |
| A | LYS18 |
| A | THR65 |
| A | TRP66 |
| A | THR67 |
| A | THR68 |
| A | HOH683 |
| A | HOH677 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 3 |
| Chain | Residue |
| A | GLU52 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 4 |
| Chain | Residue |
| A | HIS298 |
| A | ASP302 |
| A | ASP473 |
| A | HOH765 |
| A | HOH657 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 5 |
| Chain | Residue |
| B | TYR24 |
| B | GLY64 |
| B | THR68 |
| B | VAL69 |
| B | ASP72 |
| B | LEU77 |
| B | HOH694 |
| B | HOH686 |
| B | HOH620 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 6 |
| Chain | Residue |
| B | LYS18 |
| B | THR65 |
| B | THR67 |
| B | THR68 |
| B | HOH684 |
| B | HOH686 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 7 |
| Chain | Residue |
| B | GLU52 |
| B | HOH634 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 8 |
| Chain | Residue |
| B | LYS466 |
| B | PHE467 |
| B | GLU468 |
| B | PHE469 |
| B | HOH617 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 9 |
| Chain | Residue |
| B | ARG295 |
| B | GLU336 |
| B | PHE345 |
| B | ASP473 |
| B | HOH772 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 10 |
| Chain | Residue |
| E | HOH655 |
| E | TYR24 |
| E | GLY64 |
| E | THR68 |
| E | VAL69 |
| E | ASP72 |
| E | HOH667 |
| E | HOH692 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 11 |
| Chain | Residue |
| E | GLY16 |
| E | LYS18 |
| E | THR65 |
| E | TRP66 |
| E | THR67 |
| E | THR68 |
| E | HOH674 |
| E | HOH667 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 12 |
| Chain | Residue |
| B | HOH634 |
| E | LYS466 |
| E | GLU468 |
| E | PHE469 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 13 |
| Chain | Residue |
| E | HOH753 |
| E | HOH605 |
| E | ARG295 |
| E | ASP473 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 14 |
| Chain | Residue |
| A | TYR226 |
| A | ALA230 |
| F | HOH322 |
| F | HOH323 |
| F | LYS49 |
| F | GLU55 |
| F | ASP69 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 15 |
| Chain | Residue |
| F | GLY37 |
| F | TRP38 |
| F | ILE39 |
| F | GLY82 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 16 |
| Chain | Residue |
| H | HOH727 |
| H | HOH607 |
| H | LEU270 |
| V | LEU270 |
| site_id | CC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 18 |
| Chain | Residue |
| H | HOH606 |
| H | VAL17 |
| H | LYS18 |
| H | TRP66 |
| H | THR67 |
| H | THR68 |
| H | HOH689 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 19 |
| Chain | Residue |
| H | HOH768 |
| H | GLU52 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 20 |
| Chain | Residue |
| H | HOH736 |
| H | LYS466 |
| H | GLU468 |
| H | PHE469 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 21 |
| Chain | Residue |
| H | HOH776 |
| H | ARG295 |
| H | GLU336 |
| H | ASP473 |
| site_id | DC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 22 |
| Chain | Residue |
| K | EDO504 |
| K | HOH621 |
| K | HOH692 |
| K | TYR24 |
| K | THR68 |
| K | VAL69 |
| K | ASP72 |
| K | HOH682 |
| site_id | DC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 23 |
| Chain | Residue |
| K | EDO503 |
| K | HOH661 |
| K | HOH692 |
| K | VAL17 |
| K | LYS18 |
| K | THR65 |
| K | TRP66 |
| K | THR67 |
| K | THR68 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 24 |
| Chain | Residue |
| P | GLY37 |
| P | TRP38 |
| P | ILE39 |
| P | GLY82 |
| P | CYS83 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 25 |
| Chain | Residue |
| O | EDO504 |
| O | HOH652 |
| O | TYR24 |
| O | GLY64 |
| O | THR68 |
| O | VAL69 |
| O | ASP72 |
| O | HOH703 |
| O | HOH639 |
| site_id | DC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 26 |
| Chain | Residue |
| O | EDO503 |
| O | HOH652 |
| O | LYS18 |
| O | THR65 |
| O | TRP66 |
| O | THR67 |
| O | THR68 |
| O | HOH649 |
| site_id | DC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 27 |
| Chain | Residue |
| A | PHE469 |
| A | HOH619 |
| O | GLU52 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 28 |
| Chain | Residue |
| O | HOH604 |
| O | LYS466 |
| O | PHE467 |
| O | GLU468 |
| O | PHE469 |
| site_id | EC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 29 |
| Chain | Residue |
| B | TYR226 |
| T | LYS49 |
| T | GLU55 |
| T | SER56 |
| T | ASP69 |
| site_id | EC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 30 |
| Chain | Residue |
| R | HOH689 |
| K | LEU270 |
| R | LEU270 |
| R | HOH725 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 31 |
| Chain | Residue |
| B | LEU270 |
| B | HOH675 |
| B | HOH681 |
| E | LEU270 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 32 |
| Chain | Residue |
| A | LEU270 |
| A | HOH736 |
| A | HOH651 |
| O | LEU270 |
| site_id | EC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 33 |
| Chain | Residue |
| R | HOH654 |
| R | LYS18 |
| R | THR65 |
| R | TRP66 |
| R | THR67 |
| R | THR68 |
| R | HOH684 |
| site_id | EC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 34 |
| Chain | Residue |
| R | GLU52 |
| site_id | EC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 35 |
| Chain | Residue |
| R | HOH671 |
| R | LYS466 |
| R | PHE467 |
| R | GLU468 |
| R | PHE469 |
| site_id | EC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 36 |
| Chain | Residue |
| V | HOH737 |
| V | HOH659 |
| V | TYR24 |
| V | GLY64 |
| V | THR68 |
| V | VAL69 |
| V | ASP72 |
| V | LEU77 |
| V | HOH638 |
| site_id | FC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 37 |
| Chain | Residue |
| V | HOH659 |
| V | GLY16 |
| V | VAL17 |
| V | LYS18 |
| V | THR65 |
| V | THR67 |
| V | THR68 |
| V | HOH624 |
| site_id | FC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 38 |
| Chain | Residue |
| V | GLU52 |
| site_id | FC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 39 |
| Chain | Residue |
| V | HOH669 |
| V | LYS466 |
| V | PHE467 |
| V | GLU468 |
| V | PHE469 |
| V | HOH774 |
| site_id | FC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 40 |
| Chain | Residue |
| V | HOH804 |
| V | GLY337 |
| V | GLU338 |
| V | VAL341 |
| V | ASP473 |
| site_id | FC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 41 |
| Chain | Residue |
| J | GLY37 |
| J | TRP38 |
| J | ILE39 |
| J | GLY82 |
| site_id | FC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 42 |
| Chain | Residue |
| A | ALA11 |
| A | HOH778 |
| M | GLY37 |
| M | ARG84 |
| site_id | FC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 43 |
| Chain | Residue |
| T | GLY37 |
| T | TRP38 |
| T | ILE39 |
| T | PHE81 |
| T | GLY82 |
| T | CYS83 |
| site_id | FC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 44 |
| Chain | Residue |
| A | LYS466 |
| A | GLU468 |
| A | PHE469 |
| A | HOH619 |
| A | HOH748 |
| site_id | FC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 45 |
| Chain | Residue |
| R | HOH671 |
| K | TYR20 |
| K | GLU52 |
| site_id | GC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 46 |
| Chain | Residue |
| K | HOH660 |
| K | LYS466 |
| K | GLU468 |
| K | PHE469 |
| site_id | GC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 47 |
| Chain | Residue |
| K | GLU336 |
| K | ASP473 |
| K | HOH679 |
| site_id | GC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 48 |
| Chain | Residue |
| B | HOH617 |
| E | GLU52 |
| E | ALA129 |
| site_id | GC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 49 |
| Chain | Residue |
| I | HOH328 |
| I | LYS49 |
| I | GLU55 |
| I | HOH322 |
| K | TYR226 |
| K | ALA230 |
| site_id | GC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 50 |
| Chain | Residue |
| I | GLY37 |
| I | TRP38 |
| I | ILE39 |
| I | PHE81 |
| I | GLY82 |
| site_id | GC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 51 |
| Chain | Residue |
| P | HOH339 |
| P | LYS49 |
| P | GLU55 |
| P | HOH307 |
| V | TYR226 |
| site_id | GC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 52 |
| Chain | Residue |
| B | ALA11 |
| B | HOH732 |
| B | HOH837 |
| W | ARG84 |
| site_id | GC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 53 |
| Chain | Residue |
| H | HOH698 |
| H | TYR24 |
| H | THR68 |
| H | VAL69 |
| H | ASP72 |
| H | LEU77 |
| H | HOH689 |
| H | HOH730 |
| site_id | GC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 54 |
| Chain | Residue |
| R | HOH654 |
| R | HOH683 |
| R | TYR24 |
| R | GLY64 |
| R | THR68 |
| R | VAL69 |
| R | ASP72 |
| R | HOH715 |
| site_id | HC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 56 |
| Chain | Residue |
| R | HOH735 |
| R | ARG295 |
| R | GLU336 |
| R | ASP473 |
| R | HOH691 |
| site_id | HC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 57 |
| Chain | Residue |
| O | ARG295 |
| O | GLU336 |
| O | PHE345 |
| O | ASP473 |
| O | HOH782 |
| O | HOH671 |
| site_id | HC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 58 |
| Chain | Residue |
| C | LYS49 |
| C | GLU55 |
| C | SER56 |
| C | ASP69 |
| C | HOH319 |
| C | HOH336 |
| H | TYR226 |
| H | LYS227 |
| site_id | HC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 59 |
| Chain | Residue |
| C | GLY37 |
| C | TRP38 |
| C | GLY82 |
| site_id | HC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 61 |
| Chain | Residue |
| J | LYS49 |
| J | GLU55 |
| J | HOH306 |
| R | TYR226 |
| R | ALA230 |
| site_id | HC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 62 |
| Chain | Residue |
| M | LYS49 |
| M | GLU55 |
| M | HOH318 |
| O | TYR226 |
| site_id | HC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CAP E 477 |
| Chain | Residue |
| B | GLU60 |
| B | THR65 |
| B | TRP66 |
| B | ASN123 |
| B | HOH722 |
| B | HOH695 |
| 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 | MG501 |
| E | HOH639 |
| E | HOH634 |
| E | HOH646 |
| E | HOH606 |
| E | HOH700 |
| E | HOH696 |
| E | HOH608 |
| site_id | HC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CAP H 477 |
| Chain | Residue |
| 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 | MG501 |
| H | HOH633 |
| H | HOH669 |
| H | HOH651 |
| H | HOH611 |
| H | HOH665 |
| H | HOH640 |
| V | GLU60 |
| V | THR65 |
| V | TRP66 |
| V | ASN123 |
| V | HOH721 |
| V | HOH727 |
| V | HOH726 |
| site_id | HC9 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CAP K 477 |
| Chain | Residue |
| K | THR173 |
| K | LYS175 |
| K | LYS177 |
| K | KCX201 |
| K | ASP203 |
| K | GLU204 |
| K | HIS294 |
| K | ARG295 |
| K | HIS327 |
| K | LYS334 |
| K | LEU335 |
| K | SER379 |
| K | GLY380 |
| K | GLY381 |
| K | GLY403 |
| K | GLY404 |
| K | MG501 |
| K | HOH670 |
| K | HOH674 |
| K | HOH685 |
| K | HOH676 |
| K | HOH720 |
| K | HOH626 |
| R | GLU60 |
| R | THR65 |
| R | TRP66 |
| R | ASN123 |
| R | HOH644 |
| R | HOH711 |
| R | HOH639 |
| site_id | IC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CAP O 477 |
| Chain | Residue |
| A | GLU60 |
| A | THR65 |
| A | TRP66 |
| A | ASN123 |
| A | HOH744 |
| O | THR173 |
| O | LYS175 |
| O | LYS177 |
| O | KCX201 |
| O | ASP203 |
| O | GLU204 |
| O | HIS294 |
| O | ARG295 |
| O | HIS327 |
| O | LYS334 |
| O | LEU335 |
| O | SER379 |
| O | GLY380 |
| O | GLY381 |
| O | GLY403 |
| O | GLY404 |
| O | MG501 |
| O | HOH707 |
| O | HOH717 |
| O | HOH695 |
| O | HOH631 |
| O | HOH613 |
| O | HOH607 |
| O | HOH668 |
| O | HOH603 |
| site_id | IC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP R 477 |
| Chain | Residue |
| K | GLU60 |
| K | THR65 |
| K | TRP66 |
| K | ASN123 |
| K | HOH693 |
| R | THR173 |
| R | LYS175 |
| R | LYS177 |
| R | KCX201 |
| R | ASP203 |
| R | GLU204 |
| R | HIS294 |
| R | ARG295 |
| R | HIS327 |
| R | LYS334 |
| R | LEU335 |
| R | SER379 |
| R | GLY380 |
| R | GLY381 |
| R | GLY403 |
| R | GLY404 |
| R | MG501 |
| R | HOH627 |
| R | HOH625 |
| R | HOH655 |
| R | HOH702 |
| R | HOH696 |
| R | HOH667 |
| site_id | IC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP V 477 |
| Chain | Residue |
| H | GLU60 |
| H | THR65 |
| H | TRP66 |
| H | ASN123 |
| V | THR173 |
| V | LYS175 |
| V | LYS177 |
| V | KCX201 |
| V | ASP203 |
| V | GLU204 |
| V | HIS294 |
| V | ARG295 |
| V | HIS327 |
| V | LYS334 |
| V | LEU335 |
| V | SER379 |
| V | GLY380 |
| V | GLY381 |
| V | GLY403 |
| V | GLY404 |
| V | MG501 |
| V | HOH697 |
| V | HOH686 |
| V | HOH648 |
| V | HOH631 |
| V | HOH751 |
| V | HOH674 |
| V | HOH699 |
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 | 16 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in homodimeric partner"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11866526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11866526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"4-hydroxyproline","evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11866526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11866526","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6302265","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"S-methylcysteine","evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11866526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N-methylmethionine","evidences":[{"source":"PubMed","id":"11641402","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | LYS175 | |
| A | HIS294 | |
| A | LYS177 | |
| A | ASP203 | |
| A | HIS327 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | LYS175 | |
| B | HIS294 | |
| B | LYS177 | |
| B | ASP203 | |
| B | HIS327 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| E | LYS175 | |
| E | HIS294 | |
| E | LYS177 | |
| E | ASP203 | |
| E | HIS327 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| H | LYS175 | |
| H | HIS294 | |
| H | LYS177 | |
| H | ASP203 | |
| H | HIS327 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| K | LYS175 | |
| K | HIS294 | |
| K | LYS177 | |
| K | ASP203 | |
| K | HIS327 |
| site_id | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| O | LYS175 | |
| O | HIS294 | |
| O | LYS177 | |
| O | ASP203 | |
| O | HIS327 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| R | LYS175 | |
| R | HIS294 | |
| R | LYS177 | |
| R | ASP203 | |
| R | HIS327 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| V | LYS175 | |
| V | HIS294 | |
| V | LYS177 | |
| V | ASP203 | |
| V | HIS327 |
