2QYG
Crystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustris
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0015977 | biological_process | carbon fixation |
A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0015977 | biological_process | carbon fixation |
B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0015977 | biological_process | carbon fixation |
C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0015977 | biological_process | carbon fixation |
D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000255 |
Chain | Residue | Details |
A | LYS198 | |
B | LYS198 | |
C | LYS198 | |
D | LYS198 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP200 | |
A | GLU201 | |
B | ASP200 | |
B | GLU201 | |
C | ASP200 | |
C | GLU201 | |
D | ASP200 | |
D | GLU201 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000255 |
Chain | Residue | Details |
A | LYS198 | |
B | LYS198 | |
C | LYS198 | |
D | LYS198 |