2HVG
Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
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 | 0016829 | molecular_function | lyase activity |
A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
B | 0006164 | biological_process | purine nucleotide biosynthetic process |
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 | 0016829 | molecular_function | lyase activity |
B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 601 |
Chain | Residue |
A | THR167 |
B | GLN245 |
A | HIS168 |
A | SER293 |
A | LYS299 |
A | ASN301 |
A | HOH614 |
A | HOH641 |
A | HOH705 |
A | HOH888 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 602 |
Chain | Residue |
A | LYS392 |
A | ASP398 |
A | ALA399 |
A | TYR400 |
A | HOH643 |
A | HOH776 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | HIS313 |
A | ASN316 |
A | LYS320 |
A | HOH680 |
A | HOH841 |
B | SER324 |
B | LYS325 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 604 |
Chain | Residue |
A | LYS109 |
A | GLN430 |
B | ASN395 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 605 |
Chain | Residue |
A | HIS298 |
A | LYS410 |
A | VAL411 |
A | ILE412 |
A | HOH884 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 606 |
Chain | Residue |
A | HIS160 |
A | VAL161 |
A | ARG369 |
A | HOH731 |
A | HOH779 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 607 |
Chain | Residue |
A | LYS325 |
B | HIS313 |
B | ASN316 |
B | LYS320 |
B | HOH647 |
B | HOH868 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 608 |
Chain | Residue |
B | LYS283 |
B | ILE367 |
B | ASP368 |
B | ARG369 |
B | ARG370 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 609 |
Chain | Residue |
A | ASN395 |
B | LYS109 |
B | GLN430 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 610 |
Chain | Residue |
B | HIS160 |
B | VAL161 |
B | ARG369 |
B | HOH777 |
B | HOH793 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 611 |
Chain | Residue |
A | GLU112 |
A | HOH669 |
B | LYS392 |
B | ASP398 |
B | ALA399 |
B | TYR400 |
B | HOH626 |
B | HOH766 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 612 |
Chain | Residue |
A | GLN245 |
A | HOH755 |
B | THR167 |
B | LYS299 |
B | ASN301 |
B | HOH684 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 B 613 |
Chain | Residue |
B | LYS356 |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSstMpHKvN |
Chain | Residue | Details |
A | GLY292-ASN301 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | GLU306 | |
A | LYS299 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | THR167 | |
B | HIS168 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | GLU306 | |
B | LYS299 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | THR167 | |
A | HIS168 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | HIS168 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | HIS168 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | GLU309 | |
A | LYS299 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | GLU309 | |
B | LYS299 |