3UVA
Crystal structure of L-rhamnose isomerase mutant W38F from Bacillus halodurans in complex with Mn
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008740 | molecular_function | L-rhamnose isomerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019299 | biological_process | rhamnose metabolic process |
| A | 0019301 | biological_process | rhamnose catabolic process |
| A | 0019324 | biological_process | L-lyxose metabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008740 | molecular_function | L-rhamnose isomerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019299 | biological_process | rhamnose metabolic process |
| B | 0019301 | biological_process | rhamnose catabolic process |
| B | 0019324 | biological_process | L-lyxose metabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008740 | molecular_function | L-rhamnose isomerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019299 | biological_process | rhamnose metabolic process |
| C | 0019301 | biological_process | rhamnose catabolic process |
| C | 0019324 | biological_process | L-lyxose metabolic process |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008740 | molecular_function | L-rhamnose isomerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019299 | biological_process | rhamnose metabolic process |
| D | 0019301 | biological_process | rhamnose catabolic process |
| D | 0019324 | biological_process | L-lyxose metabolic process |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 419 |
| Chain | Residue |
| A | GLU225 |
| A | ASP258 |
| A | HIS285 |
| A | ASP325 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 420 |
| Chain | Residue |
| A | LYS227 |
| A | HIS261 |
| A | ASP293 |
| A | ASP295 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 419 |
| Chain | Residue |
| B | ASP258 |
| B | HIS285 |
| B | ASP325 |
| B | GLU225 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 420 |
| Chain | Residue |
| B | HIS261 |
| B | ASP293 |
| B | ASP295 |
| B | HOH488 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 419 |
| Chain | Residue |
| C | GLU225 |
| C | ASP258 |
| C | HIS285 |
| C | ASP325 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 420 |
| Chain | Residue |
| C | ASP258 |
| C | HIS261 |
| C | ASP293 |
| C | ASP295 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 419 |
| Chain | Residue |
| D | GLU225 |
| D | ASP258 |
| D | HIS285 |
| D | ASP325 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN D 420 |
| Chain | Residue |
| D | LYS227 |
| D | HIS261 |
| D | ASP293 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00541 |
| Chain | Residue | Details |
| A | HIS261 | |
| D | HIS261 | |
| D | ASP293 | |
| D | ASP295 | |
| A | ASP293 | |
| A | ASP295 | |
| B | HIS261 | |
| B | ASP293 | |
| B | ASP295 | |
| C | HIS261 | |
| C | ASP293 | |
| C | ASP295 |
