1GIN
CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH GDP, IMP, HADACIDIN, NO3-, AND MG2+. DATA COLLECTED AT 298K (PH 6.5).
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 | NO3433 |
A | HDA438 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NO3 A 433 |
Chain | Residue |
A | ASP13 |
A | LYS16 |
A | ALA39 |
A | GLY40 |
A | HIS41 |
A | ALA223 |
A | GLN224 |
A | GDP432 |
A | MG435 |
A | HDA438 |
A | IMP440 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HDA A 438 |
Chain | Residue |
A | ASP13 |
A | GLY40 |
A | THR129 |
A | GLY298 |
A | ALA299 |
A | THR300 |
A | THR301 |
A | ARG303 |
A | ARG305 |
A | GDP432 |
A | NO3433 |
A | MG435 |
A | IMP440 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE IMP A 440 |
Chain | Residue |
A | TRP11 |
A | ASP13 |
A | ASN38 |
A | ALA39 |
A | ILE126 |
A | GLY127 |
A | THR128 |
A | THR129 |
A | ARG143 |
A | GLN224 |
A | LEU228 |
A | THR239 |
A | VAL273 |
A | GLY274 |
A | ARG303 |
A | NO3433 |
A | HDA438 |
A | HOH500 |
site_id | AC5 |
Number of Residues | 20 |
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 | ARG305 |
A | LYS331 |
A | ASP333 |
A | SER414 |
A | THR415 |
A | GLY416 |
A | NO3433 |
A | MG435 |
A | HDA438 |
A | HOH493 |
A | HOH571 |
A | HOH586 |
site_id | ASP |
Number of Residues | 3 |
Details | THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE 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 GUANINE 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 |