4EEI
Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis Complexed with AMP and Succinate
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 | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide 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 | 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 | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide 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 | 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 | 23 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | GLU62 |
| A | ILE303 |
| A | SER306 |
| A | ARG310 |
| A | EDO502 |
| A | HOH608 |
| A | HOH612 |
| A | HOH703 |
| A | HOH716 |
| A | HOH753 |
| B | ARG4 |
| A | LYS66 |
| B | TYR5 |
| B | ASN276 |
| B | HOH630 |
| B | HOH664 |
| A | HIS67 |
| A | ASP68 |
| A | SER94 |
| A | SER95 |
| A | HIS141 |
| A | GLN212 |
| A | ARG301 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | HIS67 |
| A | THR93 |
| A | SER94 |
| A | AMP501 |
| A | HOH753 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | ASP427 |
| A | VAL430 |
| A | LYS431 |
| A | ARG433 |
| A | EDO506 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | ARG216 |
| A | SER306 |
| A | GLU309 |
| A | ARG310 |
| A | HOH693 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | SER111 |
| A | TYR112 |
| A | LYS115 |
| A | HOH778 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | VAL430 |
| A | LYS431 |
| A | K503 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | ALA119 |
| A | ASP122 |
| A | SER123 |
| A | THR126 |
| A | LYS328 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ARG344 |
| A | K510 |
| A | HOH883 |
| B | ASP247 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | SER140 |
| A | MET143 |
| A | PHE144 |
| B | ASN270 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 510 |
| Chain | Residue |
| A | ASP247 |
| A | EDO508 |
| A | HOH883 |
| A | HOH888 |
| B | ASP247 |
| B | EDO514 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| A | GLN79 |
| A | HOH813 |
| B | HOH666 |
| B | HOH723 |
| B | HOH795 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| A | ASN270 |
| B | SER140 |
| B | HIS141 |
| B | MET143 |
| B | PHE144 |
| B | SIN507 |
| site_id | BC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP B 503 |
| Chain | Residue |
| A | ARG4 |
| A | TYR5 |
| A | ASN276 |
| A | HOH668 |
| A | HOH707 |
| B | LYS66 |
| B | HIS67 |
| B | ASP68 |
| B | SER94 |
| B | HIS141 |
| B | GLN212 |
| B | ARG301 |
| B | ILE303 |
| B | SER306 |
| B | ARG310 |
| B | SIN507 |
| B | HOH627 |
| B | HOH632 |
| B | HOH721 |
| B | HOH817 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| B | HOH613 |
| B | HOH635 |
| B | ASP99 |
| B | SER103 |
| B | ILE214 |
| B | ILE219 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | ARG216 |
| B | SER306 |
| B | GLU309 |
| B | ARG310 |
| B | HOH759 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | GLN337 |
| B | ARG338 |
| B | ASP339 |
| B | ILE340 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SIN B 507 |
| Chain | Residue |
| A | ASN270 |
| B | HIS67 |
| B | THR93 |
| B | SER94 |
| B | SER140 |
| B | GLN212 |
| B | EDO502 |
| B | AMP503 |
| B | HOH863 |
| B | HOH866 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 508 |
| Chain | Residue |
| A | ARG54 |
| A | GLU78 |
| A | HOH661 |
| B | LEU125 |
| B | GLU129 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 509 |
| Chain | Residue |
| A | GLU60 |
| B | LYS132 |
| B | ASP423 |
| B | ARG433 |
| B | HOH874 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 510 |
| Chain | Residue |
| B | ASP427 |
| B | VAL430 |
| B | LYS431 |
| B | ARG433 |
| B | HOH873 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 511 |
| Chain | Residue |
| B | LYS173 |
| B | ASP174 |
| B | GLY175 |
| B | LEU176 |
| B | LEU204 |
| B | PRO205 |
| B | HOH708 |
| B | HOH862 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 512 |
| Chain | Residue |
| A | HOH770 |
| B | LYS132 |
| B | GLU133 |
| B | ILE422 |
| B | ASP423 |
| B | HOH875 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 513 |
| Chain | Residue |
| A | ASP122 |
| B | GLU35 |
| B | ASP36 |
| B | ARG37 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 514 |
| Chain | Residue |
| A | K510 |
| B | ARG344 |
| B | SER347 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 515 |
| Chain | Residue |
| B | HIS358 |
| B | ARG368 |
| B | HOH682 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSstMpHKkN |
| Chain | Residue | Details |
| A | GLY261-ASN270 |
