4ZFL
Ergothioneine-biosynthetic Ntn hydrolase variant EgtC_C2A with natural substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0052699 | biological_process | ergothioneine biosynthetic process |
| A | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0052699 | biological_process | ergothioneine biosynthetic process |
| B | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| C | 0006541 | biological_process | glutamine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| C | 0052699 | biological_process | ergothioneine biosynthetic process |
| C | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| D | 0006541 | biological_process | glutamine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| D | 0052699 | biological_process | ergothioneine biosynthetic process |
| D | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| E | 0006541 | biological_process | glutamine metabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| E | 0052699 | biological_process | ergothioneine biosynthetic process |
| E | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| F | 0006541 | biological_process | glutamine metabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| F | 0052699 | biological_process | ergothioneine biosynthetic process |
| F | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| G | 0006541 | biological_process | glutamine metabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| G | 0052699 | biological_process | ergothioneine biosynthetic process |
| G | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| H | 0006541 | biological_process | glutamine metabolic process |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| H | 0052699 | biological_process | ergothioneine biosynthetic process |
| H | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| I | 0006541 | biological_process | glutamine metabolic process |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| I | 0052699 | biological_process | ergothioneine biosynthetic process |
| I | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| J | 0006541 | biological_process | glutamine metabolic process |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| J | 0052699 | biological_process | ergothioneine biosynthetic process |
| J | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| K | 0006541 | biological_process | glutamine metabolic process |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| K | 0052699 | biological_process | ergothioneine biosynthetic process |
| K | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| L | 0006541 | biological_process | glutamine metabolic process |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| L | 0052699 | biological_process | ergothioneine biosynthetic process |
| L | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue 4NK A 301 |
| Chain | Residue |
| A | ALA2 |
| A | THR91 |
| A | MET94 |
| A | GLY115 |
| A | LEU116 |
| A | VAL132 |
| A | ASP133 |
| A | SER134 |
| A | ARG164 |
| A | HOH403 |
| A | HOH412 |
| A | GLN35 |
| A | HOH427 |
| A | HOH431 |
| A | HOH467 |
| A | HOH498 |
| C | TYR30 |
| C | TRP66 |
| A | HIS37 |
| A | GLY38 |
| A | LEU39 |
| A | MET40 |
| A | ARG88 |
| A | SER89 |
| A | ALA90 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue 4NK B 301 |
| Chain | Residue |
| B | ALA2 |
| B | GLN35 |
| B | HIS37 |
| B | GLY38 |
| B | LEU39 |
| B | MET40 |
| B | ARG88 |
| B | SER89 |
| B | ALA90 |
| B | THR91 |
| B | MET94 |
| B | GLY115 |
| B | ASP133 |
| B | SER134 |
| B | ARG164 |
| B | HOH412 |
| B | HOH424 |
| B | HOH444 |
| B | HOH451 |
| B | HOH482 |
| D | TYR30 |
| D | TRP66 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK C 301 |
| Chain | Residue |
| A | TYR30 |
| A | TRP66 |
| C | ALA2 |
| C | GLN35 |
| C | HIS37 |
| C | GLY38 |
| C | LEU39 |
| C | MET40 |
| C | ARG88 |
| C | SER89 |
| C | ALA90 |
| C | THR91 |
| C | MET94 |
| C | GLY115 |
| C | LEU116 |
| C | ASP133 |
| C | SER134 |
| C | ARG164 |
| C | HOH402 |
| C | HOH408 |
| C | HOH450 |
| C | HOH477 |
| C | HOH478 |
| C | HOH484 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue 4NK D 301 |
| Chain | Residue |
| B | TRP66 |
| D | ALA2 |
| D | GLN35 |
| D | HIS37 |
| D | GLY38 |
| D | LEU39 |
| D | MET40 |
| D | ARG88 |
| D | SER89 |
| D | ALA90 |
| D | THR91 |
| D | MET94 |
| D | GLY115 |
| D | ASP133 |
| D | SER134 |
| D | ARG164 |
| D | HOH405 |
| D | HOH415 |
| D | HOH447 |
| D | HOH498 |
| D | HOH506 |
| D | HOH521 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue 4NK E 301 |
| Chain | Residue |
| E | ARG88 |
| E | SER89 |
| E | ALA90 |
| E | THR91 |
| E | MET94 |
| E | GLY115 |
| E | VAL132 |
| E | ASP133 |
| E | SER134 |
| E | ARG164 |
| E | HOH406 |
| E | HOH416 |
| E | HOH418 |
| E | HOH436 |
| E | HOH484 |
| E | HOH487 |
| K | TRP66 |
| E | ALA2 |
| E | GLN35 |
| E | HIS37 |
| E | GLY38 |
| E | LEU39 |
| E | MET40 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL E 302 |
| Chain | Residue |
| E | TRP109 |
| E | GLY145 |
| E | LEU146 |
| E | ASP147 |
| E | HOH408 |
| E | HOH450 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK F 301 |
| Chain | Residue |
| F | ALA2 |
| F | GLN35 |
| F | HIS37 |
| F | GLY38 |
| F | LEU39 |
| F | MET40 |
| F | ARG88 |
| F | SER89 |
| F | ALA90 |
| F | THR91 |
| F | MET94 |
| F | GLY115 |
| F | LEU116 |
| F | ASP133 |
| F | SER134 |
| F | ARG164 |
| F | HOH401 |
| F | HOH442 |
| F | HOH443 |
| F | HOH454 |
| F | HOH474 |
| F | HOH497 |
| F | HOH573 |
| L | TRP66 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK G 301 |
| Chain | Residue |
| G | ALA2 |
| G | GLN35 |
| G | HIS37 |
| G | GLY38 |
| G | LEU39 |
| G | MET40 |
| G | ARG88 |
| G | SER89 |
| G | ALA90 |
| G | THR91 |
| G | MET94 |
| G | GLY115 |
| G | LEU116 |
| G | ASP133 |
| G | SER134 |
| G | ARG164 |
| G | HOH411 |
| G | HOH437 |
| G | HOH444 |
| G | HOH461 |
| G | HOH478 |
| G | HOH528 |
| I | TYR30 |
| I | TRP66 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL G 302 |
| Chain | Residue |
| G | TRP109 |
| G | GLY145 |
| G | LEU146 |
| G | ASP147 |
| G | HOH450 |
| site_id | AD1 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK H 301 |
| Chain | Residue |
| H | ALA2 |
| H | GLN35 |
| H | HIS37 |
| H | GLY38 |
| H | LEU39 |
| H | MET40 |
| H | ARG88 |
| H | SER89 |
| H | ALA90 |
| H | THR91 |
| H | MET94 |
| H | GLY115 |
| H | LEU116 |
| H | ASP133 |
| H | SER134 |
| H | ARG164 |
| H | HOH406 |
| H | HOH418 |
| H | HOH434 |
| H | HOH439 |
| H | HOH479 |
| H | HOH503 |
| J | TYR30 |
| J | TRP66 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK I 301 |
| Chain | Residue |
| G | TYR30 |
| G | TRP66 |
| I | ALA2 |
| I | GLN35 |
| I | HIS37 |
| I | GLY38 |
| I | LEU39 |
| I | MET40 |
| I | ARG88 |
| I | SER89 |
| I | ALA90 |
| I | THR91 |
| I | GLY115 |
| I | VAL132 |
| I | ASP133 |
| I | SER134 |
| I | ARG164 |
| I | HOH451 |
| I | HOH457 |
| I | HOH459 |
| I | HOH497 |
| I | HOH533 |
| I | HOH550 |
| I | HOH583 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL I 302 |
| Chain | Residue |
| I | GLN108 |
| I | TRP109 |
| I | GLY145 |
| I | LEU146 |
| I | ASP147 |
| I | HOH422 |
| I | HOH441 |
| I | HOH499 |
| site_id | AD4 |
| Number of Residues | 27 |
| Details | binding site for residue 4NK J 301 |
| Chain | Residue |
| H | TYR30 |
| H | TRP66 |
| J | ALA2 |
| J | GLN35 |
| J | HIS37 |
| J | GLY38 |
| J | LEU39 |
| J | MET40 |
| J | ARG88 |
| J | SER89 |
| J | ALA90 |
| J | THR91 |
| J | MET94 |
| J | ASN114 |
| J | GLY115 |
| J | LEU116 |
| J | VAL132 |
| J | ASP133 |
| J | SER134 |
| J | ARG164 |
| J | HOH402 |
| J | HOH413 |
| J | HOH428 |
| J | HOH466 |
| J | HOH469 |
| J | HOH476 |
| J | HOH531 |
| site_id | AD5 |
| Number of Residues | 24 |
| Details | binding site for residue 4NK K 301 |
| Chain | Residue |
| E | TYR30 |
| E | TRP66 |
| K | ALA2 |
| K | GLN35 |
| K | HIS37 |
| K | GLY38 |
| K | LEU39 |
| K | MET40 |
| K | ARG88 |
| K | SER89 |
| K | ALA90 |
| K | THR91 |
| K | MET94 |
| K | GLY115 |
| K | LEU116 |
| K | ASP133 |
| K | SER134 |
| K | ARG164 |
| K | HOH408 |
| K | HOH413 |
| K | HOH431 |
| K | HOH435 |
| K | HOH451 |
| K | HOH470 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL K 302 |
| Chain | Residue |
| K | GLN108 |
| K | TRP109 |
| K | GLY145 |
| K | LEU146 |
| K | ASP147 |
| K | HOH465 |
| K | HOH517 |
| site_id | AD7 |
| Number of Residues | 25 |
| Details | binding site for residue 4NK L 301 |
| Chain | Residue |
| F | TYR30 |
| F | TRP66 |
| L | ALA2 |
| L | GLN35 |
| L | HIS37 |
| L | GLY38 |
| L | LEU39 |
| L | MET40 |
| L | ARG88 |
| L | SER89 |
| L | ALA90 |
| L | THR91 |
| L | MET94 |
| L | GLY115 |
| L | LEU116 |
| L | ASP133 |
| L | SER134 |
| L | ARG164 |
| L | HOH407 |
| L | HOH412 |
| L | HOH429 |
| L | HOH456 |
| L | HOH458 |
| L | HOH494 |
| L | HOH510 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00609 |
| Chain | Residue | Details |
| A | ALA2 | |
| J | ALA2 | |
| K | ALA2 | |
| L | ALA2 | |
| B | ALA2 | |
| C | ALA2 | |
| D | ALA2 | |
| E | ALA2 | |
| F | ALA2 | |
| G | ALA2 | |
| H | ALA2 | |
| I | ALA2 |
