3BV6
Crystal structure of uncharacterized metallo protein from Vibrio cholerae with beta-lactamase like fold
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019854 | biological_process | L-ascorbic acid catabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019854 | biological_process | L-ascorbic acid catabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019854 | biological_process | L-ascorbic acid catabolic process |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019854 | biological_process | L-ascorbic acid catabolic process |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0019854 | biological_process | L-ascorbic acid catabolic process |
| E | 0030145 | molecular_function | manganese ion binding |
| E | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0019854 | biological_process | L-ascorbic acid catabolic process |
| F | 0030145 | molecular_function | manganese ion binding |
| F | 0035460 | molecular_function | L-ascorbate 6-phosphate lactonase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | HIS117 |
| A | HIS119 |
| A | ASP184 |
| A | ASP227 |
| A | HOH452 |
| A | HOH533 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 402 |
| Chain | Residue |
| A | HIS282 |
| A | HOH452 |
| A | HOH572 |
| A | ASP121 |
| A | HIS122 |
| A | ASP227 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | ASP121 |
| B | HIS122 |
| B | ASP227 |
| B | HIS282 |
| B | HOH643 |
| B | HOH773 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 402 |
| Chain | Residue |
| B | HIS117 |
| B | HIS119 |
| B | ASP184 |
| B | ASP227 |
| B | HOH643 |
| B | HOH644 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 401 |
| Chain | Residue |
| C | HIS117 |
| C | HIS119 |
| C | ASP184 |
| C | ASP227 |
| C | HOH417 |
| C | HOH784 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 402 |
| Chain | Residue |
| C | ASP121 |
| C | HIS122 |
| C | ASP227 |
| C | HIS282 |
| C | HOH417 |
| C | HOH785 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 401 |
| Chain | Residue |
| D | HIS117 |
| D | HIS119 |
| D | ASP184 |
| D | ASP227 |
| D | HOH731 |
| D | HOH739 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 402 |
| Chain | Residue |
| D | ASP121 |
| D | HIS122 |
| D | ASP227 |
| D | HIS282 |
| D | HOH731 |
| D | HOH875 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE E 401 |
| Chain | Residue |
| E | HIS117 |
| E | HIS119 |
| E | ASP184 |
| E | ASP227 |
| E | HOH877 |
| E | HOH1067 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE E 402 |
| Chain | Residue |
| E | ASP121 |
| E | HIS122 |
| E | ASP227 |
| E | HIS282 |
| E | HOH1067 |
| E | HOH1068 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE F 401 |
| Chain | Residue |
| F | HIS117 |
| F | HIS119 |
| F | ASP184 |
| F | ASP227 |
| F | HOH630 |
| F | HOH745 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE F 402 |
| Chain | Residue |
| F | ASP121 |
| F | HIS122 |
| F | ASP227 |
| F | HIS282 |
| F | HOH601 |
| F | HOH630 |
