4LF1
Hexameric Form II RuBisCO from Rhodopseudomonas palustris, activated and complexed with 2-CABP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| 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 | 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 | 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 | 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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE CAP A 800 |
| Chain | Residue |
| A | ILE165 |
| A | LYS330 |
| A | SER369 |
| A | GLY370 |
| A | GLY371 |
| A | GLY394 |
| A | GLY395 |
| A | MG801 |
| A | HOH931 |
| A | HOH933 |
| A | HOH936 |
| A | LYS167 |
| A | HOH953 |
| A | HOH954 |
| B | GLU49 |
| B | THR54 |
| B | ASN112 |
| A | LYS169 |
| A | KCX192 |
| A | ASP194 |
| A | GLU195 |
| A | HIS288 |
| A | ARG289 |
| A | HIS322 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | KCX192 |
| A | ASP194 |
| A | GLU195 |
| A | CAP800 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP B 800 |
| Chain | Residue |
| A | THR54 |
| A | ASN112 |
| B | ILE165 |
| B | LYS167 |
| B | LYS169 |
| B | KCX192 |
| B | ASP194 |
| B | GLU195 |
| B | HIS288 |
| B | ARG289 |
| B | HIS322 |
| B | LYS330 |
| B | MET331 |
| B | SER369 |
| B | GLY370 |
| B | GLY371 |
| B | GLY394 |
| B | GLY395 |
| B | MG801 |
| B | HOH929 |
| B | HOH944 |
| B | HOH946 |
| B | HOH978 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 801 |
| Chain | Residue |
| A | ASN112 |
| B | KCX192 |
| B | ASP194 |
| B | GLU195 |
| B | CAP800 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP C 800 |
| Chain | Residue |
| C | ILE165 |
| C | LYS167 |
| C | LYS169 |
| C | KCX192 |
| C | ASP194 |
| C | GLU195 |
| C | HIS288 |
| C | ARG289 |
| C | HIS322 |
| C | LYS330 |
| C | SER369 |
| C | GLY370 |
| C | GLY371 |
| C | GLY394 |
| C | GLY395 |
| C | MG801 |
| C | HOH939 |
| C | HOH946 |
| C | HOH961 |
| C | HOH962 |
| C | HOH963 |
| C | HOH966 |
| D | GLU49 |
| D | THR54 |
| D | ASN112 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 801 |
| Chain | Residue |
| C | LYS167 |
| C | KCX192 |
| C | ASP194 |
| C | GLU195 |
| C | CAP800 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP D 800 |
| Chain | Residue |
| D | LYS330 |
| D | SER369 |
| D | GLY370 |
| D | GLY371 |
| D | GLY394 |
| D | GLY395 |
| D | MG801 |
| D | HOH932 |
| D | HOH953 |
| D | HOH954 |
| D | HOH955 |
| D | HOH956 |
| C | GLU49 |
| C | THR54 |
| C | ASN112 |
| C | HOH918 |
| D | ILE165 |
| D | LYS167 |
| D | LYS169 |
| D | KCX192 |
| D | ASP194 |
| D | GLU195 |
| D | HIS288 |
| D | ARG289 |
| D | HIS322 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 801 |
| Chain | Residue |
| D | LYS167 |
| D | LYS169 |
| D | KCX192 |
| D | ASP194 |
| D | GLU195 |
| D | CAP800 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE CAP E 800 |
| Chain | Residue |
| E | ILE165 |
| E | LYS167 |
| E | LYS169 |
| E | KCX192 |
| E | ASP194 |
| E | GLU195 |
| E | HIS288 |
| E | ARG289 |
| E | HIS322 |
| E | LYS330 |
| E | MET331 |
| E | SER369 |
| E | GLY370 |
| E | GLY371 |
| E | GLY394 |
| E | GLY395 |
| E | MG801 |
| E | HOH944 |
| E | HOH946 |
| E | HOH951 |
| E | HOH959 |
| F | GLU49 |
| F | THR54 |
| F | ASN112 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 801 |
| Chain | Residue |
| E | KCX192 |
| E | ASP194 |
| E | GLU195 |
| E | CAP800 |
| site_id | BC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP F 800 |
| Chain | Residue |
| E | GLU49 |
| E | THR54 |
| E | ASN112 |
| F | ILE165 |
| F | LYS167 |
| F | LYS169 |
| F | KCX192 |
| F | ASP194 |
| F | GLU195 |
| F | HIS288 |
| F | ARG289 |
| F | HIS322 |
| F | LYS330 |
| F | SER369 |
| F | GLY370 |
| F | GLY371 |
| F | GLY394 |
| F | GLY395 |
| F | MG801 |
| F | HOH961 |
| F | HOH963 |
| F | HOH972 |
| F | HOH978 |
| F | HOH979 |
| F | HOH982 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 801 |
| Chain | Residue |
| F | KCX192 |
| F | ASP194 |
| F | GLU195 |
| F | CAP800 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE |
| Chain | Residue | Details |
| A | GLY187-GLU195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| A | LYS167 | |
| A | HIS288 | |
| B | LYS167 | |
| B | HIS288 | |
| C | LYS167 | |
| C | HIS288 | |
| D | LYS167 | |
| D | HIS288 | |
| E | LYS167 | |
| E | HIS288 | |
| F | LYS167 | |
| F | HIS288 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| A | ASN112 | |
| B | ASN112 | |
| C | ASN112 | |
| D | ASN112 | |
| E | ASN112 | |
| F | ASN112 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| C | LYS169 | |
| C | ASP194 | |
| C | GLU195 | |
| C | ARG289 | |
| C | HIS322 | |
| C | SER369 | |
| D | LYS169 | |
| D | ASP194 | |
| D | GLU195 | |
| D | ARG289 | |
| D | HIS322 | |
| D | SER369 | |
| E | LYS169 | |
| E | ASP194 | |
| E | GLU195 | |
| E | ARG289 | |
| E | HIS322 | |
| E | SER369 | |
| F | LYS169 | |
| F | ASP194 | |
| F | GLU195 | |
| F | ARG289 | |
| F | HIS322 | |
| F | SER369 | |
| A | LYS169 | |
| A | ASP194 | |
| A | GLU195 | |
| A | ARG289 | |
| A | HIS322 | |
| A | SER369 | |
| B | LYS169 | |
| B | ASP194 | |
| B | GLU195 | |
| B | ARG289 | |
| B | HIS322 | |
| B | SER369 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| A | KCX192 | |
| B | KCX192 | |
| C | KCX192 | |
| D | KCX192 | |
| E | KCX192 | |
| F | KCX192 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| A | LYS330 | |
| B | LYS330 | |
| C | LYS330 | |
| D | LYS330 | |
| E | LYS330 | |
| F | LYS330 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01339 |
| Chain | Residue | Details |
| A | KCX192 | |
| B | KCX192 | |
| C | KCX192 | |
| D | KCX192 | |
| E | KCX192 | |
| F | KCX192 |
