1CG1
STRUCTURE OF THE MUTANT (K16Q) OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH HADACIDIN, GDP, 6-PHOSPHORYL-IMP, AND MG2+
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 | HDA437 |
| A | IMO440 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HDA A 437 |
| Chain | Residue |
| A | VAL273 |
| A | GLY298 |
| A | ALA299 |
| A | THR300 |
| A | THR301 |
| A | ARG303 |
| A | ARG305 |
| A | GDP432 |
| A | MG435 |
| A | IMO440 |
| A | ASP13 |
| A | ASN38 |
| A | GLY40 |
| A | THR129 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE IMO A 440 |
| Chain | Residue |
| A | TRP11 |
| A | GLY12 |
| A | ASP13 |
| A | GLN16 |
| A | ASN38 |
| A | ALA39 |
| A | GLY40 |
| A | HIS41 |
| A | GLY127 |
| A | THR128 |
| A | THR129 |
| A | ARG143 |
| A | ALA223 |
| A | GLN224 |
| A | VAL238 |
| A | THR239 |
| A | VAL273 |
| A | GLY274 |
| A | ARG303 |
| A | GDP432 |
| A | MG435 |
| A | HDA437 |
| A | HOH532 |
| A | HOH575 |
| A | HOH632 |
| A | HOH647 |
| A | HOH651 |
| A | HOH678 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDP A 432 |
| Chain | Residue |
| A | ASP13 |
| A | GLU14 |
| A | GLY15 |
| A | GLN16 |
| A | GLY17 |
| A | LYS18 |
| A | GLY40 |
| A | HIS41 |
| A | THR42 |
| A | ARG305 |
| A | LYS331 |
| A | ASP333 |
| A | SER414 |
| A | THR415 |
| A | GLY416 |
| A | PRO417 |
| A | MG435 |
| A | HDA437 |
| A | IMO440 |
| A | HOH503 |
| A | HOH689 |
| A | HOH693 |
Functional Information from PROSITE/UniProt
| site_id | PS00513 |
| Number of Residues | 12 |
| Details | ADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYedKvaR |
| Chain | Residue | Details |
| A | GLY132-ARG143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8961938","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10346917","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9000627","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
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 | ASP13 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | GLN16 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY40 | metal ligand |
| A | HIS41 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLN224 | electrostatic stabiliser, hydrogen bond donor |
