4NAS
The crystal structure of a rubisco-like protein (MtnW) from Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
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 | 0019509 | biological_process | obsolete L-methionine salvage from methylthioadenosine |
| A | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019509 | biological_process | obsolete L-methionine salvage from methylthioadenosine |
| B | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0015977 | biological_process | carbon fixation |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019509 | biological_process | obsolete L-methionine salvage from methylthioadenosine |
| C | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0015977 | biological_process | carbon fixation |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0019509 | biological_process | obsolete L-methionine salvage from methylthioadenosine |
| D | 0043715 | molecular_function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | VAL243 |
| A | HOH603 |
| A | HOH622 |
| B | VAL243 |
| B | GLY246 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 502 |
| Chain | Residue |
| B | VAL220 |
| A | ASP248 |
| A | ALA251 |
| A | ASP252 |
| B | PRO219 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | KCX175 |
| A | ASP177 |
| A | GLU178 |
| A | HOH720 |
| A | HOH728 |
| A | HOH729 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 504 |
| Chain | Residue |
| A | PRO123 |
| A | HOH790 |
| A | HOH791 |
| A | HOH792 |
| A | HOH793 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT B 501 |
| Chain | Residue |
| B | TRP407 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 502 |
| Chain | Residue |
| B | GLU225 |
| B | GLU232 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | KCX175 |
| B | ASP177 |
| B | GLU178 |
| B | HOH727 |
| B | HOH746 |
| B | HOH794 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | PRO123 |
| B | HOH784 |
| B | HOH795 |
| B | HOH800 |
| B | HOH801 |
| B | HOH802 |
| B | HOH803 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| B | SER276 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 501 |
| Chain | Residue |
| C | KCX175 |
| C | ASP177 |
| C | GLU178 |
| C | HOH724 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 502 |
| Chain | Residue |
| C | PRO123 |
| C | HOH728 |
| C | HOH732 |
| C | HOH733 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 501 |
| Chain | Residue |
| D | KCX175 |
| D | ASP177 |
| D | GLU178 |
| D | HOH705 |
