4LF2
Hexameric Form II RuBisCO from Rhodopseudomonas palustris, activated and complexed with sulfate and magnesium
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | LYS167 |
A | KCX192 |
A | ASP194 |
A | GLU195 |
B | ASN112 |
B | HOH828 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 602 |
Chain | Residue |
A | SER369 |
A | HOH701 |
A | HOH702 |
A | HOH911 |
B | HOH847 |
A | ARG289 |
A | HIS322 |
A | MET331 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | ILE165 |
A | LYS167 |
A | LYS330 |
A | GLY371 |
A | GLY394 |
A | GLY395 |
A | HOH788 |
A | HOH813 |
B | THR54 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO3 A 604 |
Chain | Residue |
A | GLU346 |
A | HIS386 |
A | ASN388 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
A | ASN112 |
A | HOH938 |
A | HOH939 |
B | LYS167 |
B | KCX192 |
B | ASP194 |
B | GLU195 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 602 |
Chain | Residue |
A | HOH827 |
B | ARG289 |
B | HIS322 |
B | GLY324 |
B | SER369 |
B | HOH701 |
B | HOH702 |
B | HOH857 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 603 |
Chain | Residue |
A | THR54 |
B | ILE165 |
B | LYS167 |
B | LYS330 |
B | GLY371 |
B | GLY394 |
B | GLY395 |
B | HOH863 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO3 B 604 |
Chain | Residue |
B | GLU346 |
B | ASN388 |
B | HOH805 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 601 |
Chain | Residue |
C | LYS167 |
C | LYS169 |
C | KCX192 |
C | ASP194 |
C | GLU195 |
D | ASN112 |
D | HOH945 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 602 |
Chain | Residue |
C | ARG289 |
C | HIS322 |
C | SER369 |
C | HOH701 |
C | HOH702 |
C | HOH935 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 603 |
Chain | Residue |
C | LYS167 |
C | LYS330 |
C | GLY370 |
C | GLY371 |
C | GLY394 |
C | GLY395 |
D | THR54 |
D | ASN55 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO3 C 604 |
Chain | Residue |
C | GLU346 |
C | ASN388 |
C | HOH927 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 601 |
Chain | Residue |
C | ASN112 |
C | HOH953 |
D | KCX192 |
D | ASP194 |
D | GLU195 |
D | HOH944 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 D 602 |
Chain | Residue |
C | HOH869 |
D | ARG289 |
D | HIS322 |
D | SER369 |
D | HOH701 |
D | HOH702 |
D | HOH776 |
D | HOH777 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 603 |
Chain | Residue |
C | THR54 |
D | ILE165 |
D | LYS167 |
D | LYS330 |
D | GLY370 |
D | GLY371 |
D | GLY394 |
D | GLY395 |
D | HOH944 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 701 |
Chain | Residue |
E | ARG289 |
E | HIS292 |
E | HIS322 |
E | MET331 |
E | HOH801 |
E | HOH940 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 702 |
Chain | Residue |
E | LYS167 |
E | LYS330 |
E | GLY370 |
E | GLY371 |
E | GLY394 |
E | GLY395 |
E | HOH981 |
F | THR54 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 F 701 |
Chain | Residue |
E | HOH997 |
F | ARG289 |
F | HIS292 |
F | HIS322 |
F | MET331 |
F | HOH874 |
F | HOH904 |
F | HOH940 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 F 702 |
Chain | Residue |
E | THR54 |
E | ASN55 |
F | LYS167 |
F | LYS330 |
F | GLY371 |
F | GLY394 |
F | GLY395 |
F | HOH980 |
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 |