6JRQ
Crystal structure of adenylosuccinate synthetase, PurA, from Thermus thermophilus
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 | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0046040 | biological_process | IMP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004019 | molecular_function | adenylosuccinate synthase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0046040 | biological_process | IMP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004019 | molecular_function | adenylosuccinate synthase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| C | 0046040 | biological_process | IMP metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004019 | molecular_function | adenylosuccinate synthase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| D | 0046040 | biological_process | IMP metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue IMP A 501 |
| Chain | Residue |
| A | TRP11 |
| A | VAL227 |
| A | THR228 |
| A | VAL262 |
| A | HOH608 |
| A | HOH646 |
| A | HOH651 |
| A | HOH652 |
| A | HOH667 |
| A | HOH669 |
| A | HOH679 |
| A | ASP13 |
| A | HOH720 |
| B | ARG135 |
| A | ASN38 |
| A | ALA39 |
| A | GLY119 |
| A | THR120 |
| A | THR121 |
| A | GLN213 |
| A | LEU217 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | GLU26 |
| A | SER406 |
| A | TRP407 |
| D | VAL390 |
| D | ALA404 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | THR249 |
| A | ASP314 |
| B | HIS245 |
| B | LYS246 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLN10 |
| A | TRP11 |
| A | GLY12 |
| A | GLU14 |
| A | LYS256 |
| A | TYR258 |
| A | THR259 |
| A | THR260 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | VAL334 |
| A | GLU335 |
| A | ARG351 |
| A | HIS384 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue IMP B 501 |
| Chain | Residue |
| A | ARG135 |
| B | TRP11 |
| B | ASP13 |
| B | ASN38 |
| B | ALA39 |
| B | GLY119 |
| B | THR120 |
| B | THR121 |
| B | GLN213 |
| B | LEU217 |
| B | VAL227 |
| B | THR228 |
| B | VAL262 |
| B | HOH603 |
| B | HOH606 |
| B | HOH614 |
| B | HOH646 |
| B | HOH652 |
| B | HOH656 |
| B | HOH671 |
| B | HOH686 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | HIS245 |
| A | LYS246 |
| B | THR249 |
| B | LYS250 |
| B | ASP314 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | GLU26 |
| B | SER406 |
| B | TRP407 |
| C | VAL390 |
| C | ALA404 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue IMP C 501 |
| Chain | Residue |
| C | ASP13 |
| C | ASN38 |
| C | ALA39 |
| C | GLY40 |
| C | GLY119 |
| C | THR120 |
| C | THR121 |
| C | GLN213 |
| C | LEU217 |
| C | VAL227 |
| C | THR228 |
| C | VAL262 |
| C | HOH604 |
| C | HOH618 |
| C | HOH619 |
| C | HOH632 |
| C | HOH640 |
| C | HOH667 |
| C | HOH669 |
| C | HOH705 |
| D | ARG135 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | ILE248 |
| C | THR249 |
| C | ASP314 |
| D | HIS245 |
| D | LYS246 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| B | VAL390 |
| B | ALA404 |
| C | GLU26 |
| C | SER406 |
| C | TRP407 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue IMP D 501 |
| Chain | Residue |
| C | ARG135 |
| D | TRP11 |
| D | ASP13 |
| D | ASN38 |
| D | ALA39 |
| D | GLY119 |
| D | THR120 |
| D | THR121 |
| D | GLN213 |
| D | LEU217 |
| D | VAL227 |
| D | THR228 |
| D | VAL262 |
| D | GLY263 |
| D | HOH607 |
| D | HOH619 |
| D | HOH625 |
| D | HOH637 |
| D | HOH638 |
| D | HOH640 |
| D | HOH650 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| C | HIS245 |
| C | LYS246 |
| D | THR249 |
| D | ASP314 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| A | VAL390 |
| A | ALA404 |
| D | SER406 |
| D | TRP407 |
Functional Information from PROSITE/UniProt
| site_id | PS01266 |
| Number of Residues | 8 |
| Details | ADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG |
| Chain | Residue | Details |
| A | GLN10-GLY17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 88 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
