2GLX
Crystal Structure Analysis of bacterial 1,5-AF Reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0033712 | molecular_function | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1502 |
| Chain | Residue |
| A | LYS94 |
| A | HIS180 |
| A | NDP1500 |
| A | HOH1738 |
| A | HOH1846 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2502 |
| Chain | Residue |
| B | HOH2614 |
| B | HOH2624 |
| B | LYS94 |
| B | ARG163 |
| B | HIS180 |
| B | NDP2500 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT C 3502 |
| Chain | Residue |
| C | LYS94 |
| C | HIS122 |
| C | HIS180 |
| C | GLN258 |
| C | NDP3500 |
| C | HOH3573 |
| C | HOH3713 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 4502 |
| Chain | Residue |
| D | LYS94 |
| D | ARG163 |
| D | ASP176 |
| D | HIS180 |
| D | NDP4500 |
| D | HOH4580 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT E 5502 |
| Chain | Residue |
| E | LYS94 |
| E | HIS180 |
| E | NDP5500 |
| E | HOH5562 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT F 6502 |
| Chain | Residue |
| F | LYS94 |
| F | HIS180 |
| F | GLN258 |
| F | NDP6500 |
| F | HOH6511 |
| F | HOH6566 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP A 1500 |
| Chain | Residue |
| A | GLY8 |
| A | ALA9 |
| A | SER10 |
| A | THR11 |
| A | ILE12 |
| A | SER33 |
| A | THR34 |
| A | ARG38 |
| A | SER70 |
| A | THR71 |
| A | ASN73 |
| A | HIS76 |
| A | GLU93 |
| A | LYS94 |
| A | ASN120 |
| A | HIS122 |
| A | TRP162 |
| A | ARG163 |
| A | TYR283 |
| A | ACT1502 |
| A | HOH1511 |
| A | HOH1545 |
| A | HOH1552 |
| A | HOH1568 |
| A | HOH1602 |
| A | HOH1641 |
| A | HOH1648 |
| A | HOH1757 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NDP B 2500 |
| Chain | Residue |
| B | GLY8 |
| B | ALA9 |
| B | SER10 |
| B | THR11 |
| B | ILE12 |
| B | SER33 |
| B | THR34 |
| B | ARG38 |
| B | SER70 |
| B | THR71 |
| B | THR72 |
| B | ASN73 |
| B | HIS76 |
| B | GLU93 |
| B | LYS94 |
| B | ASN120 |
| B | HIS122 |
| B | LEU159 |
| B | TRP162 |
| B | ARG163 |
| B | TYR283 |
| B | ACT2502 |
| B | HOH2512 |
| B | HOH2536 |
| B | HOH2537 |
| B | HOH2599 |
| B | HOH2606 |
| B | HOH2668 |
| B | HOH2766 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP C 3500 |
| Chain | Residue |
| C | SER70 |
| C | THR71 |
| C | ASN73 |
| C | HIS76 |
| C | GLU93 |
| C | LYS94 |
| C | ASN120 |
| C | HIS122 |
| C | TRP162 |
| C | ARG163 |
| C | GLN258 |
| C | TYR283 |
| C | ACT3502 |
| C | HOH3506 |
| C | HOH3518 |
| C | HOH3530 |
| C | HOH3561 |
| C | HOH3602 |
| C | HOH3626 |
| C | HOH3663 |
| C | GLY8 |
| C | ALA9 |
| C | SER10 |
| C | THR11 |
| C | ILE12 |
| C | SER33 |
| C | THR34 |
| C | ARG38 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP D 4500 |
| Chain | Residue |
| D | GLY8 |
| D | ALA9 |
| D | SER10 |
| D | THR11 |
| D | ILE12 |
| D | SER33 |
| D | THR34 |
| D | ARG38 |
| D | SER70 |
| D | THR71 |
| D | ASN73 |
| D | HIS76 |
| D | GLU93 |
| D | LYS94 |
| D | ASN120 |
| D | TRP162 |
| D | ARG163 |
| D | ASP176 |
| D | GLN258 |
| D | TYR283 |
| D | ACT4502 |
| D | HOH4510 |
| D | HOH4525 |
| D | HOH4554 |
| site_id | BC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP E 5500 |
| Chain | Residue |
| E | GLY8 |
| E | ALA9 |
| E | SER10 |
| E | THR11 |
| E | ILE12 |
| E | SER33 |
| E | THR34 |
| E | ARG38 |
| E | SER70 |
| E | THR71 |
| E | ASN73 |
| E | HIS76 |
| E | GLU93 |
| E | LYS94 |
| E | ASN120 |
| E | HIS122 |
| E | TRP162 |
| E | ARG163 |
| E | ASP176 |
| E | GLN258 |
| E | TYR283 |
| E | ACT5502 |
| E | HOH5515 |
| E | HOH5542 |
| E | HOH5544 |
| E | HOH5599 |
| E | HOH5647 |
| E | HOH5694 |
| E | HOH5712 |
| E | HOH5717 |
| site_id | BC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP F 6500 |
| Chain | Residue |
| F | GLY8 |
| F | ALA9 |
| F | SER10 |
| F | THR11 |
| F | ILE12 |
| F | SER33 |
| F | THR34 |
| F | ARG38 |
| F | SER70 |
| F | THR71 |
| F | THR72 |
| F | ASN73 |
| F | HIS76 |
| F | GLU93 |
| F | LYS94 |
| F | ASN120 |
| F | HIS122 |
| F | LEU159 |
| F | TRP162 |
| F | ARG163 |
| F | GLN258 |
| F | TYR283 |
| F | ACT6502 |
| F | HOH6532 |
| F | HOH6580 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16906761 |
| Chain | Residue | Details |
| A | ALA9 | |
| B | SER33 | |
| B | ARG38 | |
| B | THR71 | |
| B | GLU93 | |
| B | ASN120 | |
| B | TRP162 | |
| B | TYR283 | |
| C | ALA9 | |
| C | SER33 | |
| C | ARG38 | |
| A | SER33 | |
| C | THR71 | |
| C | GLU93 | |
| C | ASN120 | |
| C | TRP162 | |
| C | TYR283 | |
| D | ALA9 | |
| D | SER33 | |
| D | ARG38 | |
| D | THR71 | |
| D | GLU93 | |
| A | ARG38 | |
| D | ASN120 | |
| D | TRP162 | |
| D | TYR283 | |
| E | ALA9 | |
| E | SER33 | |
| E | ARG38 | |
| E | THR71 | |
| E | GLU93 | |
| E | ASN120 | |
| E | TRP162 | |
| A | THR71 | |
| E | TYR283 | |
| F | ALA9 | |
| F | SER33 | |
| F | ARG38 | |
| F | THR71 | |
| F | GLU93 | |
| F | ASN120 | |
| F | TRP162 | |
| F | TYR283 | |
| A | GLU93 | |
| A | ASN120 | |
| A | TRP162 | |
| A | TYR283 | |
| B | ALA9 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ebf |
| Chain | Residue | Details |
| E | ASP192 | |
| E | ALA196 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ebf |
| Chain | Residue | Details |
| F | ASP192 | |
| F | ALA196 |
