4MX2
Crystal Structure of adenylosuccinate lyase from Leishmania donovani
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| A | 0006188 | biological_process | IMP biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| B | 0006188 | biological_process | IMP biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| C | 0006188 | biological_process | IMP biosynthetic process |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| C | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| D | 0006188 | biological_process | IMP biosynthetic process |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| D | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| E | 0006188 | biological_process | IMP biosynthetic process |
| E | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| E | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| E | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| F | 0006188 | biological_process | IMP biosynthetic process |
| F | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| F | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| F | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| G | 0006188 | biological_process | IMP biosynthetic process |
| G | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| G | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| G | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| H | 0006188 | biological_process | IMP biosynthetic process |
| H | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| H | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| H | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | ASN117 |
| A | SER366 |
| A | THR367 |
| A | ARG370 |
| A | HOH640 |
| A | HOH656 |
| A | HOH660 |
| A | HOH718 |
| B | ARG40 |
| B | TYR41 |
| B | ILE331 |
| A | HIS118 |
| B | ASN335 |
| B | HOH702 |
| E | HIS196 |
| A | ASP119 |
| A | SER149 |
| A | GLN150 |
| A | ASN153 |
| A | GLN273 |
| A | ARG361 |
| A | LEU363 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP B 501 |
| Chain | Residue |
| A | ARG40 |
| A | TYR41 |
| A | ILE331 |
| A | ASN335 |
| A | HOH713 |
| B | ASN117 |
| B | HIS118 |
| B | ASP119 |
| B | SER149 |
| B | GLN150 |
| B | GLN273 |
| B | ARG361 |
| B | LEU363 |
| B | SER366 |
| B | THR367 |
| B | ARG370 |
| B | HOH614 |
| B | HOH722 |
| B | HOH758 |
| B | HOH812 |
| B | HOH820 |
| F | HIS196 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP C 501 |
| Chain | Residue |
| C | ASN117 |
| C | HIS118 |
| C | ASP119 |
| C | SER149 |
| C | GLN150 |
| C | GLN273 |
| C | ARG361 |
| C | LEU363 |
| C | SER366 |
| C | THR367 |
| C | ARG370 |
| C | HOH617 |
| C | HOH627 |
| C | HOH648 |
| C | HOH767 |
| C | HOH779 |
| D | ARG40 |
| D | TYR41 |
| D | ILE331 |
| D | ASN335 |
| D | HOH717 |
| G | HIS196 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 502 |
| Chain | Residue |
| C | LYS121 |
| C | HIS144 |
| C | LEU147 |
| C | THR148 |
| C | SER149 |
| C | HOH647 |
| C | HOH663 |
| G | HOH795 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP D 501 |
| Chain | Residue |
| C | ARG40 |
| C | TYR41 |
| C | ASN335 |
| C | HOH692 |
| D | ASN117 |
| D | HIS118 |
| D | ASP119 |
| D | SER149 |
| D | GLN150 |
| D | ASN153 |
| D | GLN273 |
| D | ARG361 |
| D | SER366 |
| D | THR367 |
| D | ARG370 |
| D | HOH626 |
| D | HOH627 |
| D | HOH687 |
| D | HOH692 |
| D | HOH788 |
| H | HIS196 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 501 |
| Chain | Residue |
| E | ASP365 |
| E | SER366 |
| E | LEU369 |
| E | GLN150 |
| E | ASN153 |
| E | ILE157 |
| E | ARG361 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP E 502 |
| Chain | Residue |
| A | HIS196 |
| E | ASN117 |
| E | HIS118 |
| E | ASP119 |
| E | SER149 |
| E | GLN150 |
| E | GLN273 |
| E | ARG361 |
| E | SER366 |
| E | THR367 |
| E | ARG370 |
| E | HOH628 |
| E | HOH630 |
| E | HOH648 |
| E | HOH691 |
| E | HOH705 |
| F | ARG40 |
| F | TYR41 |
| F | ILE331 |
| F | ASN335 |
| F | HOH753 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP F 501 |
| Chain | Residue |
| B | HIS196 |
| E | ARG40 |
| E | TYR41 |
| E | ILE331 |
| E | ASN335 |
| E | HOH735 |
| F | ASN117 |
| F | HIS118 |
| F | ASP119 |
| F | SER149 |
| F | GLN150 |
| F | ASN153 |
| F | GLN273 |
| F | ARG361 |
| F | LEU363 |
| F | SER366 |
| F | THR367 |
| F | ARG370 |
| F | HOH618 |
| F | HOH699 |
| F | HOH770 |
| F | HOH799 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP G 501 |
| Chain | Residue |
| C | HIS196 |
| C | HOH750 |
| G | ASN117 |
| G | HIS118 |
| G | ASP119 |
| G | SER149 |
| G | GLN150 |
| G | GLN273 |
| G | ARG361 |
| G | LEU363 |
| G | SER366 |
| G | THR367 |
| G | ARG370 |
| G | HOH615 |
| G | HOH646 |
| G | HOH663 |
| H | ARG40 |
| H | TYR41 |
| H | ILE331 |
| H | ASN335 |
| H | HOH628 |
| H | HOH718 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 G 502 |
| Chain | Residue |
| G | LYS121 |
| G | HIS144 |
| G | LEU147 |
| G | THR148 |
| G | SER149 |
| G | HOH813 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE AMP H 501 |
| Chain | Residue |
| D | HIS196 |
| G | ARG40 |
| G | TYR41 |
| G | ILE331 |
| G | ASN335 |
| G | HOH728 |
| H | ASN117 |
| H | HIS118 |
| H | ASP119 |
| H | SER149 |
| H | GLN150 |
| H | GLN273 |
| H | ARG361 |
| H | LEU363 |
| H | SER366 |
| H | THR367 |
| H | ARG370 |
| H | HOH623 |
| H | HOH624 |
| H | HOH651 |
| H | HOH735 |
| H | HOH745 |
| H | HOH755 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 H 502 |
| Chain | Residue |
| H | LYS121 |
| H | HIS144 |
| H | THR148 |
| H | SER149 |
| H | HOH711 |
| H | HOH853 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMpHKvN |
| Chain | Residue | Details |
| A | GLY320-ASN329 |
