3N2C
Crystal structure of prolidase eah89906 complexed with n-methylphosphonate-l-proline
Replaces: 3LWYFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0016787 | molecular_function | hydrolase activity |
| M | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| M | 0046872 | molecular_function | metal ion binding |
| N | 0016787 | molecular_function | hydrolase activity |
| N | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| N | 0046872 | molecular_function | metal ion binding |
| O | 0016787 | molecular_function | hydrolase activity |
| O | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| O | 0046872 | molecular_function | metal ion binding |
| P | 0016787 | molecular_function | hydrolase activity |
| P | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 425 |
| Chain | Residue |
| A | HIS63 |
| A | HIS65 |
| A | KCX188 |
| A | ASP321 |
| A | LWY427 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 426 |
| Chain | Residue |
| A | KCX188 |
| A | HIS229 |
| A | HIS249 |
| A | LWY427 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY A 427 |
| Chain | Residue |
| A | HIS65 |
| A | LEU73 |
| A | HIS140 |
| A | KCX188 |
| A | GLY194 |
| A | VAL195 |
| A | ALA196 |
| A | HIS229 |
| A | TYR231 |
| A | HIS249 |
| A | ASP321 |
| A | ZN425 |
| A | ZN426 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 425 |
| Chain | Residue |
| B | HIS63 |
| B | HIS65 |
| B | KCX188 |
| B | ASP321 |
| B | LWY427 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 426 |
| Chain | Residue |
| B | KCX188 |
| B | HIS229 |
| B | HIS249 |
| B | LWY427 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY B 427 |
| Chain | Residue |
| B | HIS63 |
| B | HIS65 |
| B | LEU73 |
| B | HIS140 |
| B | KCX188 |
| B | VAL195 |
| B | ALA196 |
| B | HIS229 |
| B | TYR231 |
| B | ASP321 |
| B | ZN425 |
| B | ZN426 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 425 |
| Chain | Residue |
| C | HIS63 |
| C | HIS65 |
| C | KCX188 |
| C | ASP321 |
| C | LWY427 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 426 |
| Chain | Residue |
| C | KCX188 |
| C | HIS229 |
| C | HIS249 |
| C | LWY427 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY C 427 |
| Chain | Residue |
| C | HIS63 |
| C | HIS65 |
| C | LEU73 |
| C | HIS140 |
| C | KCX188 |
| C | VAL195 |
| C | ALA196 |
| C | HIS229 |
| C | TYR231 |
| C | HIS249 |
| C | ASP321 |
| C | ZN425 |
| C | ZN426 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 425 |
| Chain | Residue |
| D | HIS63 |
| D | HIS65 |
| D | KCX188 |
| D | ASP321 |
| D | LWY427 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 426 |
| Chain | Residue |
| D | KCX188 |
| D | HIS229 |
| D | HIS249 |
| D | LWY427 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY D 427 |
| Chain | Residue |
| D | HIS63 |
| D | HIS65 |
| D | HIS140 |
| D | KCX188 |
| D | VAL195 |
| D | ALA196 |
| D | HIS229 |
| D | TYR231 |
| D | HIS249 |
| D | TYR275 |
| D | ASP321 |
| D | ZN425 |
| D | ZN426 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 425 |
| Chain | Residue |
| E | HIS63 |
| E | HIS65 |
| E | KCX188 |
| E | ASP321 |
| E | LWY427 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 426 |
| Chain | Residue |
| E | KCX188 |
| E | HIS229 |
| E | HIS249 |
| E | LWY427 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY E 427 |
| Chain | Residue |
| E | KCX188 |
| E | VAL195 |
| E | ALA196 |
| E | HIS229 |
| E | TYR231 |
| E | HIS249 |
| E | ASP321 |
| E | ZN425 |
| E | ZN426 |
| E | HIS63 |
| E | HIS65 |
| E | HIS140 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN F 425 |
| Chain | Residue |
| F | HIS63 |
| F | HIS65 |
| F | ALA106 |
| F | KCX188 |
| F | ASP321 |
| F | LWY427 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 426 |
| Chain | Residue |
| F | KCX188 |
| F | HIS229 |
| F | HIS249 |
| F | LWY427 |
| site_id | BC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY F 427 |
| Chain | Residue |
| F | HIS63 |
| F | HIS65 |
| F | HIS140 |
| F | KCX188 |
| F | GLY194 |
| F | VAL195 |
| F | ALA196 |
| F | HIS229 |
| F | TYR231 |
| F | ASP321 |
| F | ZN425 |
| F | ZN426 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 425 |
| Chain | Residue |
| G | HIS63 |
| G | HIS65 |
| G | KCX188 |
| G | ASP321 |
| G | LWY427 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN G 426 |
| Chain | Residue |
| G | KCX188 |
| G | HIS229 |
| G | HIS249 |
| G | LWY427 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY G 427 |
| Chain | Residue |
| G | HIS63 |
| G | HIS65 |
| G | LEU73 |
| G | HIS140 |
| G | KCX188 |
| G | VAL195 |
| G | ALA196 |
| G | HIS229 |
| G | TYR231 |
| G | HIS249 |
| G | ASP321 |
| G | ZN425 |
| G | ZN426 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN H 425 |
| Chain | Residue |
| H | HIS63 |
| H | HIS65 |
| H | KCX188 |
| H | ASP321 |
| H | LWY427 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 426 |
| Chain | Residue |
| H | KCX188 |
| H | HIS229 |
| H | HIS249 |
| H | LWY427 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY H 427 |
| Chain | Residue |
| H | HIS63 |
| H | HIS65 |
| H | LEU73 |
| H | HIS140 |
| H | KCX188 |
| H | VAL195 |
| H | ALA196 |
| H | HIS229 |
| H | TYR231 |
| H | ASP321 |
| H | ZN425 |
| H | ZN426 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN I 425 |
| Chain | Residue |
| I | HIS63 |
| I | HIS65 |
| I | KCX188 |
| I | ASP321 |
| I | LWY427 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 426 |
| Chain | Residue |
| I | KCX188 |
| I | HIS229 |
| I | HIS249 |
| I | LWY427 |
| site_id | CC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LWY I 427 |
| Chain | Residue |
| I | HIS65 |
| I | LEU73 |
| I | HIS140 |
| I | KCX188 |
| I | VAL195 |
| I | ALA196 |
| I | TYR231 |
| I | HIS249 |
| I | ASP321 |
| I | ZN425 |
| I | ZN426 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN J 425 |
| Chain | Residue |
| J | HIS63 |
| J | HIS65 |
| J | KCX188 |
| J | ASP321 |
| J | LWY427 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN J 426 |
| Chain | Residue |
| J | KCX188 |
| J | HIS229 |
| J | HIS249 |
| J | LWY427 |
| site_id | DC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY J 427 |
| Chain | Residue |
| J | HIS63 |
| J | HIS65 |
| J | HIS140 |
| J | GLY194 |
| J | VAL195 |
| J | ALA196 |
| J | HIS229 |
| J | TYR231 |
| J | HIS249 |
| J | ASP321 |
| J | ZN425 |
| J | ZN426 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN K 425 |
| Chain | Residue |
| K | HIS63 |
| K | HIS65 |
| K | KCX188 |
| K | ASP321 |
| K | LWY427 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN K 426 |
| Chain | Residue |
| K | KCX188 |
| K | HIS229 |
| K | HIS249 |
| K | LWY427 |
| site_id | DC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY K 427 |
| Chain | Residue |
| K | HIS63 |
| K | HIS65 |
| K | LEU73 |
| K | HIS140 |
| K | KCX188 |
| K | VAL195 |
| K | ALA196 |
| K | HIS229 |
| K | TYR231 |
| K | HIS249 |
| K | ASP321 |
| K | ZN425 |
| K | ZN426 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN L 425 |
| Chain | Residue |
| L | HIS63 |
| L | HIS65 |
| L | KCX188 |
| L | ASP321 |
| L | LWY427 |
| site_id | DC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN L 426 |
| Chain | Residue |
| L | KCX188 |
| L | HIS229 |
| L | HIS249 |
| L | LWY427 |
| site_id | DC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY L 427 |
| Chain | Residue |
| L | HIS63 |
| L | HIS65 |
| L | LEU73 |
| L | HIS140 |
| L | KCX188 |
| L | VAL195 |
| L | ALA196 |
| L | HIS229 |
| L | TYR231 |
| L | HIS249 |
| L | ASP321 |
| L | ZN425 |
| L | ZN426 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN M 425 |
| Chain | Residue |
| M | HIS63 |
| M | HIS65 |
| M | KCX188 |
| M | ASP321 |
| M | LWY427 |
| site_id | EC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN M 426 |
| Chain | Residue |
| M | KCX188 |
| M | HIS229 |
| M | HIS249 |
| M | LWY427 |
| site_id | EC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY M 427 |
| Chain | Residue |
| M | HIS63 |
| M | HIS65 |
| M | LEU73 |
| M | HIS140 |
| M | KCX188 |
| M | VAL195 |
| M | ALA196 |
| M | HIS229 |
| M | TYR231 |
| M | HIS249 |
| M | ASP321 |
| M | ZN425 |
| M | ZN426 |
| site_id | EC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN N 425 |
| Chain | Residue |
| N | HIS63 |
| N | HIS65 |
| N | KCX188 |
| N | ASP321 |
| N | ZN426 |
| N | LWY427 |
| site_id | EC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN N 426 |
| Chain | Residue |
| N | KCX188 |
| N | HIS229 |
| N | HIS249 |
| N | ZN425 |
| N | LWY427 |
| site_id | EC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY N 427 |
| Chain | Residue |
| N | HIS63 |
| N | HIS65 |
| N | HIS140 |
| N | KCX188 |
| N | GLY194 |
| N | VAL195 |
| N | ALA196 |
| N | HIS229 |
| N | TYR231 |
| N | HIS249 |
| N | ASP321 |
| N | ZN425 |
| N | ZN426 |
| site_id | EC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN O 425 |
| Chain | Residue |
| O | HIS63 |
| O | HIS65 |
| O | KCX188 |
| O | ASP321 |
| O | LWY427 |
| site_id | EC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN O 426 |
| Chain | Residue |
| O | KCX188 |
| O | HIS229 |
| O | HIS249 |
| O | LWY427 |
| site_id | EC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LWY O 427 |
| Chain | Residue |
| O | HIS63 |
| O | HIS65 |
| O | HIS140 |
| O | KCX188 |
| O | VAL195 |
| O | ALA196 |
| O | HIS229 |
| O | TYR231 |
| O | HIS249 |
| O | ASP321 |
| O | ZN425 |
| O | ZN426 |
| site_id | FC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN P 425 |
| Chain | Residue |
| P | HIS63 |
| P | HIS65 |
| P | KCX188 |
| P | ASP321 |
| P | LWY427 |
| site_id | FC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN P 426 |
| Chain | Residue |
| P | KCX188 |
| P | HIS229 |
| P | HIS249 |
| P | LWY427 |
| site_id | FC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LWY P 427 |
| Chain | Residue |
| P | HIS63 |
| P | HIS65 |
| P | HIS140 |
| P | KCX188 |
| P | GLY194 |
| P | VAL195 |
| P | ALA196 |
| P | HIS229 |
| P | TYR231 |
| P | HIS249 |
| P | ASP321 |
| P | ZN425 |
| P | ZN426 |
