2PTQ
Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP and fumarate
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 | 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 | 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 | 13 |
| Details | BINDING SITE FOR RESIDUE FUM B 1100 |
| Chain | Residue |
| A | HIS91 |
| B | SER296 |
| B | MET298 |
| B | LYS301 |
| B | ASN303 |
| A | THR122 |
| A | SER123 |
| A | THR170 |
| A | ASN171 |
| A | GLN247 |
| A | AMP2200 |
| A | HOH2211 |
| B | SER295 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FUM A 1200 |
| Chain | Residue |
| A | SER295 |
| A | SER296 |
| A | MET298 |
| A | LYS301 |
| A | ASN303 |
| B | HIS91 |
| B | THR122 |
| B | SER123 |
| B | THR170 |
| B | ASN171 |
| B | GLN247 |
| B | AMP2100 |
| B | HOH2128 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE AMP B 2100 |
| Chain | Residue |
| A | ARG15 |
| A | TYR16 |
| A | ASN303 |
| A | ILE305 |
| A | ASN309 |
| A | FUM1200 |
| B | GLU86 |
| B | ASN90 |
| B | HIS91 |
| B | ASP92 |
| B | SER123 |
| B | GLU124 |
| B | ASN171 |
| B | GLN247 |
| B | ARG335 |
| B | LEU337 |
| B | SER340 |
| B | THR341 |
| B | ARG344 |
| B | HOH2119 |
| B | HOH2128 |
| B | HOH2171 |
| B | HOH2192 |
| B | HOH2242 |
| B | HOH2243 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE AMP A 2200 |
| Chain | Residue |
| A | ASN90 |
| A | HIS91 |
| A | ASP92 |
| A | SER123 |
| A | GLU124 |
| A | ASN171 |
| A | GLN247 |
| A | ARG335 |
| A | LEU337 |
| A | SER340 |
| A | THR341 |
| A | ARG344 |
| A | HOH2211 |
| A | HOH2249 |
| A | HOH2257 |
| A | HOH2270 |
| A | HOH2327 |
| A | HOH2414 |
| B | ARG15 |
| B | TYR16 |
| B | ASN303 |
| B | ILE305 |
| B | ASN309 |
| B | FUM1100 |
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 | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17531264 |
| Chain | Residue | Details |
| A | ASN171 | |
| A | SER295 | |
| B | ASN171 | |
| B | SER295 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTR |
| Chain | Residue | Details |
| A | ARG15 | |
| B | ARG15 | |
| B | ASN90 | |
| B | THR122 | |
| B | GLN247 | |
| B | SER296 | |
| B | LYS301 | |
| B | ASN309 | |
| B | ARG335 | |
| B | SER340 | |
| A | ASN90 | |
| A | THR122 | |
| A | GLN247 | |
| A | SER296 | |
| A | LYS301 | |
| A | ASN309 | |
| A | ARG335 | |
| A | SER340 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTQ |
| Chain | Residue | Details |
| A | HIS91 | |
| B | HIS91 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS94 | |
| A | LYS366 | |
| B | LYS94 | |
| B | LYS366 |
