1MEZ
Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with SAMP, GDP, SO4(2-), and Mg(2+)
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 | 0006541 | biological_process | glutamine metabolic process |
A | 0014850 | biological_process | response to muscle activity |
A | 0016020 | cellular_component | membrane |
A | 0016874 | molecular_function | ligase activity |
A | 0042594 | biological_process | response to starvation |
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 |
A | 0071257 | biological_process | cellular response to electrical stimulus |
A | 0071466 | biological_process | cellular response to xenobiotic stimulus |
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 | GDP1452 |
A | SO41454 |
A | 2SA1455 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 1454 |
Chain | Residue |
A | GLY70 |
A | HIS71 |
A | ALA255 |
A | ASN256 |
A | GDP1452 |
A | MG1453 |
A | 2SA1455 |
A | GLY42 |
A | ASP43 |
A | LYS46 |
A | ALA69 |
site_id | AC3 |
Number of Residues | 24 |
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 | VAL331 |
A | ARG337 |
A | LYS363 |
A | ASP365 |
A | ILE366 |
A | GLY445 |
A | VAL446 |
A | GLY447 |
A | LYS448 |
A | HOH504 |
A | HOH529 |
A | HOH553 |
A | MG1453 |
A | SO41454 |
A | 2SA1455 |
site_id | AC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE 2SA A 1455 |
Chain | Residue |
A | TRP41 |
A | ASP43 |
A | ASN68 |
A | GLY70 |
A | THR162 |
A | THR163 |
A | ARG177 |
A | ASN256 |
A | LEU260 |
A | VAL270 |
A | THR271 |
A | VAL305 |
A | GLY330 |
A | VAL331 |
A | THR332 |
A | THR333 |
A | ARG335 |
A | ARG337 |
A | HOH515 |
A | HOH532 |
A | HOH559 |
A | HOH613 |
A | GDP1452 |
A | MG1453 |
A | SO41454 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03126 |
Chain | Residue | Details |
A | ASP43 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03126 |
Chain | Residue | Details |
A | HIS71 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071 |
Chain | Residue | Details |
A | GLY42 | |
A | ARG177 | |
A | ARG337 | |
A | LYS363 | |
A | GLY445 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP43 | |
A | GLY70 | |
A | VAL331 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: in other chain |
Chain | Residue | Details |
A | ASN68 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071 |
Chain | Residue | Details |
A | THR163 | |
A | ASN256 | |
A | THR271 | |
A | ARG335 |