2OEM
Crystal structure of a rubisco-like protein from Geobacillus kaustophilus liganded with Mg2+ and 2,3-diketohexane 1-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| A | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 911 |
| Chain | Residue |
| A | KCX173 |
| A | ASP175 |
| A | GLU176 |
| A | 1AE901 |
| A | HOH1189 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 912 |
| Chain | Residue |
| B | HOH1225 |
| B | HOH1233 |
| B | KCX173 |
| B | ASP175 |
| B | GLU176 |
| B | HOH1003 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 1AE A 901 |
| Chain | Residue |
| A | ILE145 |
| A | LYS147 |
| A | KCX173 |
| A | ASP175 |
| A | GLU176 |
| A | HIS264 |
| A | ALA336 |
| A | GLY337 |
| A | ALA358 |
| A | GLY359 |
| A | GLY360 |
| A | MG911 |
| A | HOH966 |
| A | HOH978 |
| A | HOH1191 |
| B | LYS98 |
| B | HOH1235 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AE B 902 |
| Chain | Residue |
| A | LYS98 |
| B | GLY337 |
| B | ALA358 |
| B | GLY359 |
| B | GLY360 |
| B | GLY361 |
| B | HOH1132 |
| B | HOH1169 |
| B | HOH1227 |
| B | HOH1228 |
| B | HOH1230 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"17352497","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
