1UWA
L290F mutant rubisco from chlamydomonas
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 | 0009536 | cellular_component | plastid |
A | 0009853 | biological_process | photorespiration |
A | 0015977 | biological_process | carbon fixation |
A | 0015979 | biological_process | photosynthesis |
A | 0016491 | molecular_function | oxidoreductase activity |
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 | 0009536 | cellular_component | plastid |
B | 0009853 | biological_process | photorespiration |
B | 0015977 | biological_process | carbon fixation |
B | 0015979 | biological_process | photosynthesis |
B | 0016491 | molecular_function | oxidoreductase activity |
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 |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0004497 | molecular_function | monooxygenase activity |
E | 0009507 | cellular_component | chloroplast |
E | 0009536 | cellular_component | plastid |
E | 0009853 | biological_process | photorespiration |
E | 0015977 | biological_process | carbon fixation |
E | 0015979 | biological_process | photosynthesis |
E | 0016491 | molecular_function | oxidoreductase activity |
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 |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0004497 | molecular_function | monooxygenase activity |
H | 0009507 | cellular_component | chloroplast |
H | 0009536 | cellular_component | plastid |
H | 0009853 | biological_process | photorespiration |
H | 0015977 | biological_process | carbon fixation |
H | 0015979 | biological_process | photosynthesis |
H | 0016491 | molecular_function | oxidoreductase activity |
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 |
K | 0000287 | molecular_function | magnesium ion binding |
K | 0004497 | molecular_function | monooxygenase activity |
K | 0009507 | cellular_component | chloroplast |
K | 0009536 | cellular_component | plastid |
K | 0009853 | biological_process | photorespiration |
K | 0015977 | biological_process | carbon fixation |
K | 0015979 | biological_process | photosynthesis |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016829 | molecular_function | lyase activity |
K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
K | 0019253 | biological_process | reductive pentose-phosphate cycle |
K | 0046872 | molecular_function | metal ion binding |
O | 0000287 | molecular_function | magnesium ion binding |
O | 0004497 | molecular_function | monooxygenase activity |
O | 0009507 | cellular_component | chloroplast |
O | 0009536 | cellular_component | plastid |
O | 0009853 | biological_process | photorespiration |
O | 0015977 | biological_process | carbon fixation |
O | 0015979 | biological_process | photosynthesis |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016829 | molecular_function | lyase activity |
O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
O | 0019253 | biological_process | reductive pentose-phosphate cycle |
O | 0046872 | molecular_function | metal ion binding |
R | 0000287 | molecular_function | magnesium ion binding |
R | 0004497 | molecular_function | monooxygenase activity |
R | 0009507 | cellular_component | chloroplast |
R | 0009536 | cellular_component | plastid |
R | 0009853 | biological_process | photorespiration |
R | 0015977 | biological_process | carbon fixation |
R | 0015979 | biological_process | photosynthesis |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0016829 | molecular_function | lyase activity |
R | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
R | 0019253 | biological_process | reductive pentose-phosphate cycle |
R | 0046872 | molecular_function | metal ion binding |
V | 0000287 | molecular_function | magnesium ion binding |
V | 0004497 | molecular_function | monooxygenase activity |
V | 0009507 | cellular_component | chloroplast |
V | 0009536 | cellular_component | plastid |
V | 0009853 | biological_process | photorespiration |
V | 0015977 | biological_process | carbon fixation |
V | 0015979 | biological_process | photosynthesis |
V | 0016491 | molecular_function | oxidoreductase activity |
V | 0016829 | molecular_function | lyase activity |
V | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
V | 0019253 | biological_process | reductive pentose-phosphate cycle |
V | 0046872 | molecular_function | metal ion binding |
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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS175 | |
K | HIS294 | |
O | LYS175 | |
O | HIS294 | |
R | LYS175 | |
R | HIS294 | |
V | LYS175 | |
V | HIS294 | |
A | HIS294 | |
B | LYS175 | |
B | HIS294 | |
E | LYS175 | |
E | HIS294 | |
H | LYS175 | |
H | HIS294 | |
K | LYS175 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in homodimeric partner |
Chain | Residue | Details |
A | ASN123 | |
B | ASN123 | |
E | ASN123 | |
H | ASN123 | |
K | ASN123 | |
O | ASN123 | |
R | ASN123 | |
V | ASN123 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | BINDING: |
Chain | Residue | Details |
A | THR173 | |
B | SER379 | |
E | THR173 | |
E | LYS177 | |
E | ARG295 | |
E | HIS327 | |
E | SER379 | |
H | THR173 | |
H | LYS177 | |
H | ARG295 | |
H | HIS327 | |
A | LYS177 | |
H | SER379 | |
K | THR173 | |
K | LYS177 | |
K | ARG295 | |
K | HIS327 | |
K | SER379 | |
O | THR173 | |
O | LYS177 | |
O | ARG295 | |
O | HIS327 | |
A | ARG295 | |
O | SER379 | |
R | THR173 | |
R | LYS177 | |
R | ARG295 | |
R | HIS327 | |
R | SER379 | |
V | THR173 | |
V | LYS177 | |
V | ARG295 | |
V | HIS327 | |
A | HIS327 | |
V | SER379 | |
A | SER379 | |
B | THR173 | |
B | LYS177 | |
B | ARG295 | |
B | HIS327 |
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 | |
E | KCX201 | |
H | KCX201 | |
K | KCX201 | |
O | KCX201 | |
R | KCX201 | |
V | 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 | |
K | GLU204 | |
O | ASP203 | |
O | GLU204 | |
R | ASP203 | |
R | GLU204 | |
V | ASP203 | |
V | GLU204 | |
A | GLU204 | |
B | ASP203 | |
B | GLU204 | |
E | ASP203 | |
E | GLU204 | |
H | ASP203 | |
H | GLU204 | |
K | ASP203 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS334 | |
B | LYS334 | |
E | LYS334 | |
H | LYS334 | |
K | LYS334 | |
O | LYS334 | |
R | LYS334 | |
V | 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 | |
E | PRO3 | |
H | PRO3 | |
K | PRO3 | |
O | PRO3 | |
R | PRO3 | |
V | 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 | |
K | HYP151 | |
O | HYP104 | |
O | HYP151 | |
R | HYP104 | |
R | HYP151 | |
V | HYP104 | |
V | HYP151 | |
A | HYP151 | |
B | HYP104 | |
B | HYP151 | |
E | HYP104 | |
E | HYP151 | |
H | HYP104 | |
H | HYP151 | |
K | HYP104 |
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 | |
E | KCX201 | |
H | KCX201 | |
K | KCX201 | |
O | KCX201 | |
R | KCX201 | |
V | 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 | |
K | SMC369 | |
O | SMC256 | |
O | SMC369 | |
R | SMC256 | |
R | SMC369 | |
V | SMC256 | |
V | SMC369 | |
A | SMC369 | |
B | SMC256 | |
B | SMC369 | |
E | SMC256 | |
E | SMC369 | |
H | SMC256 | |
H | SMC369 | |
K | SMC256 |
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 |