6KYJ
Hybrid-Rubisco (rice RbcL and sorghum RbcS) in complex with sulfate ions
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 | 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 |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0009507 | cellular_component | chloroplast |
C | 0009536 | cellular_component | plastid |
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 |
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 | 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 |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0004497 | molecular_function | monooxygenase activity |
G | 0009507 | cellular_component | chloroplast |
G | 0009536 | cellular_component | plastid |
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 |
S | 0009507 | cellular_component | chloroplast |
S | 0009853 | biological_process | photorespiration |
S | 0015977 | biological_process | carbon fixation |
S | 0015979 | biological_process | photosynthesis |
S | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
S | 0019253 | biological_process | reductive pentose-phosphate cycle |
U | 0009507 | cellular_component | chloroplast |
U | 0009853 | biological_process | photorespiration |
U | 0015977 | biological_process | carbon fixation |
U | 0015979 | biological_process | photosynthesis |
U | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
U | 0019253 | biological_process | reductive pentose-phosphate cycle |
W | 0009507 | cellular_component | chloroplast |
W | 0009853 | biological_process | photorespiration |
W | 0015977 | biological_process | carbon fixation |
W | 0015979 | biological_process | photosynthesis |
W | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
W | 0019253 | biological_process | reductive pentose-phosphate cycle |
Y | 0009507 | cellular_component | chloroplast |
Y | 0009853 | biological_process | photorespiration |
Y | 0015977 | biological_process | carbon fixation |
Y | 0015979 | biological_process | photosynthesis |
Y | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
Y | 0019253 | biological_process | reductive pentose-phosphate cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | TRP66 |
A | GLY381 |
A | GLY403 |
A | GLY404 |
A | HOH621 |
A | HOH711 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | HOH641 |
A | HOH748 |
A | ARG295 |
A | HIS298 |
A | GLY329 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ARG134 |
A | LYS305 |
A | HIS310 |
A | MET341 |
A | HOH698 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | THR26 |
A | LYS81 |
A | ARG83 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 505 |
Chain | Residue |
A | ASN442 |
A | ARG446 |
A | HOH808 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 506 |
Chain | Residue |
A | LYS356 |
A | PHE364 |
A | THR365 |
A | HOH786 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | LYS146 |
A | PHE148 |
A | HOH615 |
A | HOH645 |
A | HOH781 |
E | GLU110 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | LYS227 |
A | GLU231 |
A | HOH696 |
A | HOH759 |
S | TYR7 |
W | PHE44 |
W | SER45 |
W | TRP66 |
W | THR67 |
W | HOH210 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue GOL A 509 |
Chain | Residue |
A | GLU433 |
A | ARG435 |
S | GLN25 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue SO4 E 501 |
Chain | Residue |
E | LYS175 |
E | GLY381 |
E | GLY403 |
E | GLY404 |
E | HOH614 |
E | HOH681 |
G | TRP66 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue SO4 E 502 |
Chain | Residue |
E | ARG295 |
E | HIS298 |
E | GLY329 |
G | HOH757 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SO4 E 503 |
Chain | Residue |
E | ARG134 |
E | LYS305 |
E | HIS310 |
E | MET341 |
E | HOH655 |
E | HOH731 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue SO4 E 504 |
Chain | Residue |
E | THR26 |
E | LYS81 |
E | ARG83 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue SO4 E 505 |
Chain | Residue |
E | ASN442 |
E | GLU443 |
E | ARG446 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue GOL E 506 |
Chain | Residue |
A | GLU110 |
E | LYS146 |
E | PHE148 |
E | HOH602 |
E | HOH604 |
E | HOH665 |
E | HOH714 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for residue GOL E 507 |
Chain | Residue |
E | TYR190 |
E | LYS227 |
E | GLU231 |
E | HOH601 |
E | HOH741 |
U | SER45 |
U | TRP66 |
U | THR67 |
U | HOH205 |
W | TYR7 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue GOL E 508 |
Chain | Residue |
E | GLU433 |
E | ARG435 |
W | GLN25 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 501 |
Chain | Residue |
C | TRP66 |
C | GLY381 |
C | GLY403 |
C | GLY404 |
C | HOH617 |
C | HOH620 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 502 |
Chain | Residue |
C | ARG295 |
C | HIS298 |
C | GLY329 |
C | HOH608 |
C | HOH754 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 503 |
Chain | Residue |
C | ARG134 |
C | LYS305 |
C | HIS310 |
C | MET341 |
C | HOH645 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 504 |
Chain | Residue |
C | THR26 |
C | LYS81 |
C | ARG83 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 505 |
Chain | Residue |
C | ASN442 |
C | ARG446 |
site_id | AE5 |
Number of Residues | 7 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
C | SER145 |
C | LYS146 |
C | PHE148 |
C | HOH624 |
C | HOH680 |
C | HOH704 |
G | GLU110 |
site_id | AE6 |
Number of Residues | 10 |
Details | binding site for residue GOL C 507 |
Chain | Residue |
C | LYS227 |
C | GLU231 |
C | HOH610 |
C | HOH621 |
C | HOH740 |
U | TYR7 |
Y | PHE44 |
Y | SER45 |
Y | TRP66 |
Y | THR67 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue GOL C 508 |
Chain | Residue |
C | GLU433 |
C | ARG435 |
U | GLN25 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue SO4 G 501 |
Chain | Residue |
E | TRP66 |
G | GLY381 |
G | GLY403 |
G | GLY404 |
G | HOH607 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue SO4 G 502 |
Chain | Residue |
G | ARG295 |
G | HIS298 |
G | GLY329 |
site_id | AF1 |
Number of Residues | 5 |
Details | binding site for residue SO4 G 503 |
Chain | Residue |
G | ARG134 |
G | LYS305 |
G | HIS310 |
G | MET341 |
G | HOH665 |
site_id | AF2 |
Number of Residues | 3 |
Details | binding site for residue SO4 G 504 |
Chain | Residue |
G | THR26 |
G | LYS81 |
G | ARG83 |
site_id | AF3 |
Number of Residues | 2 |
Details | binding site for residue SO4 G 505 |
Chain | Residue |
G | ASN442 |
G | ARG446 |
site_id | AF4 |
Number of Residues | 7 |
Details | binding site for residue GOL G 506 |
Chain | Residue |
C | GLU110 |
G | LYS146 |
G | PHE148 |
G | HOH605 |
G | HOH640 |
G | HOH657 |
G | HOH722 |
site_id | AF5 |
Number of Residues | 10 |
Details | binding site for residue GOL G 507 |
Chain | Residue |
G | TYR190 |
G | LYS227 |
G | GLU231 |
G | HOH624 |
G | HOH649 |
G | HOH743 |
S | SER45 |
S | TRP66 |
S | THR67 |
Y | TYR7 |
site_id | AF6 |
Number of Residues | 3 |
Details | binding site for residue GOL G 508 |
Chain | Residue |
G | GLN149 |
G | ASP286 |
G | HOH640 |
site_id | AF7 |
Number of Residues | 5 |
Details | binding site for residue GOL G 509 |
Chain | Residue |
E | LEU270 |
E | ILE301 |
E | HOH740 |
G | LEU270 |
G | HOH761 |
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 | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | LYS175 | |
A | HIS294 | |
E | LYS175 | |
E | HIS294 | |
C | LYS175 | |
C | HIS294 | |
G | LYS175 | |
G | HIS294 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: in homodimeric partner => ECO:0000250 |
Chain | Residue | Details |
A | ASN123 | |
E | ASN123 | |
C | ASN123 | |
G | ASN123 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | THR173 | |
E | ASP203 | |
E | GLU204 | |
E | ARG295 | |
E | HIS327 | |
E | SER379 | |
C | THR173 | |
C | LYS177 | |
C | ASP203 | |
C | GLU204 | |
C | ARG295 | |
A | LYS177 | |
C | HIS327 | |
C | SER379 | |
G | THR173 | |
G | LYS177 | |
G | ASP203 | |
G | GLU204 | |
G | ARG295 | |
G | HIS327 | |
G | SER379 | |
A | ASP203 | |
A | GLU204 | |
A | ARG295 | |
A | HIS327 | |
A | SER379 | |
E | THR173 | |
E | LYS177 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000250 |
Chain | Residue | Details |
A | LYS201 | |
E | LYS201 | |
C | LYS201 | |
G | LYS201 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | LYS334 | |
E | LYS334 | |
C | LYS334 | |
G | LYS334 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylproline => ECO:0000250 |
Chain | Residue | Details |
A | PRO3 | |
E | PRO3 | |
C | PRO3 | |
G | PRO3 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS201 | |
E | LYS201 | |
C | LYS201 | |
G | LYS201 |