1LNY
Crystal structure of the recombinant mouse-muscle adenylosuccinate synthetase complexed with 6-phosphoryl-IMP, GDP and Mg
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0004019 | molecular_function | adenylosuccinate synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006163 | biological_process | purine nucleotide metabolic process |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006167 | biological_process | AMP biosynthetic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046040 | biological_process | IMP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051015 | molecular_function | actin filament binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0004019 | molecular_function | adenylosuccinate synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006163 | biological_process | purine nucleotide metabolic process |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006167 | biological_process | AMP biosynthetic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0044209 | biological_process | AMP salvage |
| B | 0046040 | biological_process | IMP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1453 |
| Chain | Residue |
| A | ASP43 |
| A | GLY70 |
| A | HOH817 |
| A | IMO1451 |
| A | GDP1452 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1456 |
| Chain | Residue |
| B | IMO1455 |
| B | ASP43 |
| B | GLY70 |
| B | HOH696 |
| B | GDP1454 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE IMO A 1451 |
| Chain | Residue |
| A | TRP41 |
| A | GLY42 |
| A | ASP43 |
| A | LYS46 |
| A | ASN68 |
| A | ALA69 |
| A | GLY70 |
| A | HIS71 |
| A | GLY161 |
| A | THR162 |
| A | THR163 |
| A | ASN256 |
| A | LEU260 |
| A | VAL270 |
| A | THR271 |
| A | VAL305 |
| A | GLY306 |
| A | ARG335 |
| A | HOH501 |
| A | HOH602 |
| A | HOH649 |
| A | HOH660 |
| A | HOH703 |
| A | HOH817 |
| A | GDP1452 |
| A | MG1453 |
| B | ARG177 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP A 1452 |
| Chain | Residue |
| A | ASP43 |
| A | GLU44 |
| A | GLY45 |
| A | LYS46 |
| A | GLY47 |
| A | LYS48 |
| A | GLY70 |
| A | HIS71 |
| A | THR72 |
| A | LYS363 |
| A | ASP365 |
| A | GLY445 |
| A | VAL446 |
| A | GLY447 |
| A | LYS448 |
| A | HOH581 |
| A | HOH645 |
| A | HOH817 |
| A | IMO1451 |
| A | MG1453 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 1454 |
| Chain | Residue |
| B | ASP43 |
| B | GLU44 |
| B | GLY45 |
| B | LYS46 |
| B | GLY47 |
| B | LYS48 |
| B | GLY70 |
| B | HIS71 |
| B | THR72 |
| B | LYS363 |
| B | ASP365 |
| B | GLY445 |
| B | VAL446 |
| B | GLY447 |
| B | LYS448 |
| B | HOH594 |
| B | HOH710 |
| B | IMO1455 |
| B | MG1456 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE IMO B 1455 |
| Chain | Residue |
| B | MG1456 |
| A | ARG177 |
| B | TRP41 |
| B | GLY42 |
| B | ASP43 |
| B | LYS46 |
| B | ASN68 |
| B | ALA69 |
| B | GLY70 |
| B | HIS71 |
| B | GLY161 |
| B | THR162 |
| B | THR163 |
| B | ASN256 |
| B | LEU260 |
| B | VAL270 |
| B | THR271 |
| B | VAL305 |
| B | GLY306 |
| B | HOH514 |
| B | HOH534 |
| B | HOH577 |
| B | HOH659 |
| B | GDP1454 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03126","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_03126","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12004071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in other chain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12004071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
