1JUY
REFINED CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH HYDANTOCIDIN 5'-PHOSPHATE GDP, HPO4(2-), MG2+, AND HADACIDIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0046040 | biological_process | IMP metabolic process |
| A | 0046086 | biological_process | adenosine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 435 |
| Chain | Residue |
| A | ASP13 |
| A | GLY40 |
| A | GDP432 |
| A | PI434 |
| A | HDA438 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PI A 434 |
| Chain | Residue |
| A | GLY12 |
| A | ASP13 |
| A | LYS16 |
| A | ASN38 |
| A | ALA39 |
| A | GLY40 |
| A | HIS41 |
| A | ALA223 |
| A | GLN224 |
| A | GDP432 |
| A | H5P433 |
| A | MG435 |
| A | HDA438 |
| A | HOH661 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDP A 432 |
| Chain | Residue |
| A | ASP13 |
| A | GLU14 |
| A | GLY15 |
| A | LYS16 |
| A | GLY17 |
| A | GLY40 |
| A | HIS41 |
| A | THR42 |
| A | ALA299 |
| A | ARG305 |
| A | LYS331 |
| A | ASP333 |
| A | SER414 |
| A | THR415 |
| A | GLY416 |
| A | PRO417 |
| A | PI434 |
| A | MG435 |
| A | HDA438 |
| A | HOH552 |
| A | HOH581 |
| A | HOH631 |
| A | HOH644 |
| A | HOH712 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE H5P A 433 |
| Chain | Residue |
| A | ASN38 |
| A | GLY127 |
| A | THR128 |
| A | THR129 |
| A | ARG143 |
| A | GLN224 |
| A | LEU228 |
| A | VAL238 |
| A | THR239 |
| A | VAL273 |
| A | GLY274 |
| A | ARG303 |
| A | PI434 |
| A | HOH554 |
| A | HOH578 |
| A | HOH582 |
| A | HOH608 |
| A | HOH661 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HDA A 438 |
| Chain | Residue |
| A | ASP13 |
| A | ASN38 |
| A | GLY40 |
| A | THR129 |
| A | VAL273 |
| A | GLY298 |
| A | ALA299 |
| A | THR300 |
| A | THR301 |
| A | ARG303 |
| A | GDP432 |
| A | PI434 |
| A | MG435 |
| site_id | ASP |
| Number of Residues | 3 |
| Details | THESE RESIDUES MAKE UP THE ASPARTATE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE. |
| Chain | Residue |
| A | ARG305 |
| A | THR301 |
| A | ARG303 |
| site_id | GNS |
| Number of Residues | 13 |
| Details | THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE. |
| Chain | Residue |
| A | ASP13 |
| A | SER414 |
| A | THR415 |
| A | GLY416 |
| A | PRO417 |
| A | GLU14 |
| A | GLY15 |
| A | LYS16 |
| A | GLY17 |
| A | LYS18 |
| A | LYS331 |
| A | LEU332 |
| A | ASP333 |
| site_id | IMP |
| Number of Residues | 6 |
| Details | THESE RESIDUES MAKE UP THE INOSINE NUCLEOTIDE BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE. |
| Chain | Residue |
| A | ASN38 |
| A | THR129 |
| A | ARG143 |
| A | GLN224 |
| A | THR239 |
| A | VAL273 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU14 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | THR42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917 |
| Chain | Residue | Details |
| A | ASP13 | |
| A | ARG306 | |
| A | LEU332 | |
| A | THR415 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938, ECO:0000269|PubMed:9000627 |
| Chain | Residue | Details |
| A | GLU14 | |
| A | HIS41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: in other chain |
| Chain | Residue | Details |
| A | ALA39 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627 |
| Chain | Residue | Details |
| A | GLY130 | |
| A | GLY225 | |
| A | SER240 | |
| A | ARG304 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011, ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627 |
| Chain | Residue | Details |
| A | ARG144 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR300 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1gim |
| Chain | Residue | Details |
| A | ASP13 | |
| A | GLN224 | |
| A | HIS41 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 65 |
| Chain | Residue | Details |
| A | GLU14 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | GLY17 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS41 | metal ligand |
| A | THR42 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY225 | electrostatic stabiliser, hydrogen bond donor |
