2PTR
Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate
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 | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006163 | biological_process | purine nucleotide metabolic process |
| 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 | 0006974 | biological_process | DNA damage response |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006163 | biological_process | purine nucleotide metabolic process |
| 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 | 0006974 | biological_process | DNA damage response |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE 2SA B 1100 |
| Chain | Residue |
| A | ARG15 |
| A | ASN309 |
| B | GLU86 |
| B | ASN90 |
| B | HIS91 |
| B | ASP92 |
| B | THR122 |
| B | SER123 |
| B | GLU124 |
| B | THR170 |
| B | GLN247 |
| A | TYR16 |
| B | ARG335 |
| B | LEU337 |
| B | SER340 |
| B | THR341 |
| B | ARG344 |
| B | HOH1226 |
| B | HOH1229 |
| B | HOH1231 |
| B | HOH1313 |
| B | HOH1315 |
| A | GLY294 |
| B | HOH1317 |
| A | SER295 |
| A | SER296 |
| A | THR297 |
| A | MET298 |
| A | LYS301 |
| A | ASN303 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 2SA B 1200 |
| Chain | Residue |
| A | ASN90 |
| A | HIS91 |
| A | ASP92 |
| A | THR122 |
| A | SER123 |
| A | GLU124 |
| A | THR170 |
| A | GLN247 |
| A | ARG335 |
| A | SER340 |
| A | THR341 |
| A | ARG344 |
| A | HOH469 |
| A | HOH479 |
| A | HOH514 |
| A | HOH706 |
| B | ARG15 |
| B | TYR16 |
| B | MET298 |
| B | LYS301 |
| B | ASN303 |
| B | ASN309 |
| B | HOH1306 |
| B | HOH1342 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSstMpHKvN |
| Chain | Residue | Details |
| A | GLY294-ASN303 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17531264","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17531264","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PTR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17531264","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PTQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
