8ILB
The complexes of RbcL, AtRaf1 and AtBSD2 (LFB)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005515 | molecular_function | protein binding |
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 | 0031470 | cellular_component | carboxysome |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005515 | molecular_function | protein binding |
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 | 0031470 | cellular_component | carboxysome |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005515 | molecular_function | protein binding |
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 | 0031470 | cellular_component | carboxysome |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005515 | molecular_function | protein binding |
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 | 0031470 | cellular_component | carboxysome |
D | 0046872 | molecular_function | metal ion binding |
J | 0000287 | molecular_function | magnesium ion binding |
J | 0004497 | molecular_function | monooxygenase activity |
J | 0005515 | molecular_function | protein binding |
J | 0009853 | biological_process | photorespiration |
J | 0015977 | biological_process | carbon fixation |
J | 0015979 | biological_process | photosynthesis |
J | 0016829 | molecular_function | lyase activity |
J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
J | 0019253 | biological_process | reductive pentose-phosphate cycle |
J | 0031470 | cellular_component | carboxysome |
J | 0046872 | molecular_function | metal ion binding |
K | 0000287 | molecular_function | magnesium ion binding |
K | 0004497 | molecular_function | monooxygenase activity |
K | 0005515 | molecular_function | protein binding |
K | 0009853 | biological_process | photorespiration |
K | 0015977 | biological_process | carbon fixation |
K | 0015979 | biological_process | photosynthesis |
K | 0016829 | molecular_function | lyase activity |
K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
K | 0019253 | biological_process | reductive pentose-phosphate cycle |
K | 0031470 | cellular_component | carboxysome |
K | 0046872 | molecular_function | metal ion binding |
L | 0000287 | molecular_function | magnesium ion binding |
L | 0004497 | molecular_function | monooxygenase activity |
L | 0005515 | molecular_function | protein binding |
L | 0009853 | biological_process | photorespiration |
L | 0015977 | biological_process | carbon fixation |
L | 0015979 | biological_process | photosynthesis |
L | 0016829 | molecular_function | lyase activity |
L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
L | 0019253 | biological_process | reductive pentose-phosphate cycle |
L | 0031470 | cellular_component | carboxysome |
L | 0046872 | molecular_function | metal ion binding |
M | 0000287 | molecular_function | magnesium ion binding |
M | 0004497 | molecular_function | monooxygenase activity |
M | 0005515 | molecular_function | protein binding |
M | 0009853 | biological_process | photorespiration |
M | 0015977 | biological_process | carbon fixation |
M | 0015979 | biological_process | photosynthesis |
M | 0016829 | molecular_function | lyase activity |
M | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
M | 0019253 | biological_process | reductive pentose-phosphate cycle |
M | 0031470 | cellular_component | carboxysome |
M | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LTGISSIEQNRLIVGA |
Chain | Residue | Details |
E | LEU121-ALA136 |
site_id | PS00157 |
Number of Residues | 9 |
Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE |
Chain | Residue | Details |
A | GLY193-GLU201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 568 |
Details | ZN_FING: CR-type => ECO:0000255|PROSITE-ProRule:PRU00546 |
Chain | Residue | Details |
F | PRO62-THR133 | |
G | PRO62-THR133 | |
H | PRO62-THR133 | |
I | PRO62-THR133 | |
O | PRO62-THR133 | |
P | PRO62-THR133 | |
Q | PRO62-THR133 | |
R | PRO62-THR133 | |
J | LYS172 | |
J | HIS291 | |
K | LYS172 | |
K | HIS291 | |
L | LYS172 | |
L | HIS291 | |
M | LYS172 | |
M | HIS291 |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29217567, ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC |
Chain | Residue | Details |
F | CYS72 | |
F | CYS75 | |
F | CYS83 | |
F | CYS86 | |
F | CYS107 | |
F | CYS110 | |
F | CYS118 | |
F | CYS121 | |
G | CYS72 | |
G | CYS75 | |
G | CYS83 | |
G | CYS86 | |
G | CYS107 | |
G | CYS110 | |
G | CYS118 | |
G | CYS121 | |
H | CYS72 | |
H | CYS75 | |
H | CYS83 | |
H | CYS86 | |
H | CYS107 | |
H | CYS110 | |
H | CYS118 | |
H | CYS121 | |
I | CYS72 | |
I | CYS75 | |
I | CYS83 | |
I | CYS86 | |
I | CYS107 | |
I | CYS110 | |
I | CYS118 | |
I | CYS121 | |
O | CYS72 | |
O | CYS75 | |
O | CYS83 | |
O | CYS86 | |
O | CYS107 | |
O | CYS110 | |
O | CYS118 | |
O | CYS121 | |
P | CYS72 | |
P | CYS75 | |
P | CYS83 | |
P | CYS86 | |
P | CYS107 | |
P | CYS110 | |
P | CYS118 | |
P | CYS121 | |
Q | CYS72 | |
Q | CYS75 | |
Q | CYS83 | |
Q | CYS86 | |
Q | CYS107 | |
Q | CYS110 | |
Q | CYS118 | |
Q | CYS121 | |
R | CYS72 | |
R | CYS75 | |
R | CYS83 | |
R | CYS86 | |
R | CYS107 | |
R | CYS110 | |
R | CYS118 | |
R | CYS121 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29217567, ECO:0007744|PDB:6EKB |
Chain | Residue | Details |
F | GLU78 | |
F | CYS80 | |
F | GLU115 | |
G | GLU78 | |
G | CYS80 | |
G | GLU115 | |
H | GLU78 | |
H | CYS80 | |
H | GLU115 | |
I | GLU78 | |
I | CYS80 | |
I | GLU115 | |
O | GLU78 | |
O | CYS80 | |
O | GLU115 | |
P | GLU78 | |
P | CYS80 | |
P | GLU115 | |
Q | GLU78 | |
Q | CYS80 | |
Q | GLU115 | |
R | GLU78 | |
R | CYS80 | |
R | GLU115 | |
J | SER376 | |
K | THR170 | |
K | LYS174 | |
K | ARG292 | |
K | HIS324 | |
K | SER376 | |
L | THR170 | |
L | LYS174 | |
L | ARG292 | |
L | HIS324 | |
L | SER376 | |
M | THR170 | |
M | LYS174 | |
M | ARG292 | |
M | HIS324 | |
M | SER376 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:8245022 |
Chain | Residue | Details |
A | LYS198 | |
B | LYS198 | |
C | LYS198 | |
D | LYS198 | |
J | LYS198 | |
K | LYS198 | |
L | LYS198 | |
M | LYS198 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8245022 |
Chain | Residue | Details |
A | ASP200 | |
A | GLU201 | |
B | ASP200 | |
B | GLU201 | |
C | ASP200 | |
C | GLU201 | |
D | ASP200 | |
D | GLU201 | |
J | ASP200 | |
J | GLU201 | |
K | ASP200 | |
K | GLU201 | |
L | ASP200 | |
L | GLU201 | |
M | ASP200 | |
M | GLU201 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS331 | |
B | LYS331 | |
C | LYS331 | |
D | LYS331 | |
J | LYS331 | |
K | LYS331 | |
L | LYS331 | |
M | LYS331 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:16593333 |
Chain | Residue | Details |
A | LYS198 | |
B | LYS198 | |
C | LYS198 | |
D | LYS198 | |
J | LYS198 | |
K | LYS198 | |
L | LYS198 | |
M | LYS198 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
A | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
A | LYS198 | metal ligand, nucleophile, proton donor |
A | ASP200 | metal ligand |
A | GLU201 | metal ligand |
A | HIS291 | proton acceptor |
A | LYS331 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
B | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
B | LYS198 | metal ligand, nucleophile, proton donor |
B | ASP200 | metal ligand |
B | GLU201 | metal ligand |
B | HIS291 | proton acceptor |
B | LYS331 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
C | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
C | LYS198 | metal ligand, nucleophile, proton donor |
C | ASP200 | metal ligand |
C | GLU201 | metal ligand |
C | HIS291 | proton acceptor |
C | LYS331 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
D | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
D | LYS198 | metal ligand, nucleophile, proton donor |
D | ASP200 | metal ligand |
D | GLU201 | metal ligand |
D | HIS291 | proton acceptor |
D | LYS331 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
J | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
J | LYS198 | metal ligand, nucleophile, proton donor |
J | ASP200 | metal ligand |
J | GLU201 | metal ligand |
J | HIS291 | proton acceptor |
J | LYS331 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
K | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
K | LYS198 | metal ligand, nucleophile, proton donor |
K | ASP200 | metal ligand |
K | GLU201 | metal ligand |
K | HIS291 | proton acceptor |
K | LYS331 | electrostatic stabiliser |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
L | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
L | LYS198 | metal ligand, nucleophile, proton donor |
L | ASP200 | metal ligand |
L | GLU201 | metal ligand |
L | HIS291 | proton acceptor |
L | LYS331 | electrostatic stabiliser |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
M | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
M | LYS198 | metal ligand, nucleophile, proton donor |
M | ASP200 | metal ligand |
M | GLU201 | metal ligand |
M | HIS291 | proton acceptor |
M | LYS331 | electrostatic stabiliser |