2OEL
Crystal structure of a rubisco-like protein from Geobacillus kaustophilus liganded with Mg2+ and HCO3- ions
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
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 | 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 | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
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 | 7 |
Details | BINDING SITE FOR RESIDUE CO3 A 801 |
Chain | Residue |
A | ALA336 |
A | GLY337 |
A | ILE338 |
A | ALA358 |
A | GLY361 |
A | HOH935 |
A | HOH1124 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 901 |
Chain | Residue |
A | GLU176 |
A | HOH939 |
A | HOH940 |
A | HOH974 |
A | KCX173 |
A | ASP175 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CO3 B 802 |
Chain | Residue |
B | ALA336 |
B | GLY337 |
B | ILE338 |
B | ALA358 |
B | GLY361 |
B | HOH915 |
B | HOH1270 |
B | HOH1271 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 902 |
Chain | Residue |
B | KCX173 |
B | ASP175 |
B | GLU176 |
B | HOH919 |
B | HOH944 |
B | HOH957 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS98 | |
B | LYS98 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS147 | |
B | HIS264 | |
B | GLY337 | |
B | GLY359 | |
A | ASP175 | |
A | GLU176 | |
A | HIS264 | |
A | GLY337 | |
A | GLY359 | |
B | LYS147 | |
B | ASP175 | |
B | GLU176 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: via carbamate group |
Chain | Residue | Details |
A | KCX173 | |
B | KCX173 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:17352497 |
Chain | Residue | Details |
A | KCX173 | |
B | KCX173 |