1KH2
Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0000053 | biological_process | argininosuccinate metabolic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004055 | molecular_function | argininosuccinate synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| B | 0000050 | biological_process | urea cycle |
| B | 0000053 | biological_process | argininosuccinate metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004055 | molecular_function | argininosuccinate synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| C | 0000050 | biological_process | urea cycle |
| C | 0000053 | biological_process | argininosuccinate metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004055 | molecular_function | argininosuccinate synthase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| D | 0000050 | biological_process | urea cycle |
| D | 0000053 | biological_process | argininosuccinate metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004055 | molecular_function | argininosuccinate synthase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006526 | biological_process | L-arginine biosynthetic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ATP A 510 |
| Chain | Residue |
| A | ALA6 |
| A | ILE95 |
| A | HIS113 |
| A | GLY114 |
| A | ALA115 |
| A | PHE125 |
| A | SER8 |
| A | GLY10 |
| A | LEU11 |
| A | ASP12 |
| A | THR13 |
| A | PHE31 |
| A | ALA33 |
| A | GLN37 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ATP B 1510 |
| Chain | Residue |
| B | ALA6 |
| B | TYR7 |
| B | SER8 |
| B | GLY10 |
| B | ASP12 |
| B | THR13 |
| B | PHE31 |
| B | THR32 |
| B | ALA33 |
| B | GLN37 |
| B | HIS113 |
| B | GLY114 |
| B | PHE125 |
| B | HOH1380 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ATP C 2510 |
| Chain | Residue |
| C | ALA6 |
| C | TYR7 |
| C | SER8 |
| C | GLY10 |
| C | LEU11 |
| C | ASP12 |
| C | THR13 |
| C | PHE31 |
| C | THR32 |
| C | ALA33 |
| C | GLN37 |
| C | HIS113 |
| C | GLY114 |
| C | PHE125 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP D 3510 |
| Chain | Residue |
| D | ALA6 |
| D | TYR7 |
| D | SER8 |
| D | GLY10 |
| D | LEU11 |
| D | ASP12 |
| D | THR13 |
| D | PHE31 |
| D | ALA33 |
| D | ARG92 |
| D | HIS113 |
| D | GLY114 |
| D | PHE125 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00005","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11844799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12684518","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kp2 |
| Chain | Residue | Details |
| A | ASP121 | |
| A | ARG92 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kp2 |
| Chain | Residue | Details |
| B | ASP121 | |
| B | ARG92 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kp2 |
| Chain | Residue | Details |
| C | ASP121 | |
| C | ARG92 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kp2 |
| Chain | Residue | Details |
| D | ASP121 | |
| D | ARG92 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 316 |
| Chain | Residue | Details |
| A | ASP12 | steric role |
| A | ARG92 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP121 | proton acceptor, proton donor |
| A | SER173 | hydrogen bond donor, steric role |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 316 |
| Chain | Residue | Details |
| B | ASP12 | steric role |
| B | ARG92 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP121 | proton acceptor, proton donor |
| B | SER173 | hydrogen bond donor, steric role |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 316 |
| Chain | Residue | Details |
| C | ASP12 | steric role |
| C | ARG92 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP121 | proton acceptor, proton donor |
| C | SER173 | hydrogen bond donor, steric role |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 316 |
| Chain | Residue | Details |
| D | ASP12 | steric role |
| D | ARG92 | electrostatic stabiliser, hydrogen bond donor |
| D | ASP121 | proton acceptor, proton donor |
| D | SER173 | hydrogen bond donor, steric role |
