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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | TRP11 |
| A | THR238 |
| A | VAL272 |
| A | GLY273 |
| A | EDO503 |
| A | HOH607 |
| A | HOH626 |
| A | HOH657 |
| A | HOH660 |
| A | HOH782 |
| A | HOH783 |
| A | GLY12 |
| A | HOH785 |
| B | ARG142 |
| A | ASN38 |
| A | GLY126 |
| A | THR127 |
| A | THR128 |
| A | GLN223 |
| A | LEU227 |
| A | VAL237 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLI A 502 |
| Chain | Residue |
| A | GLY12 |
| A | ASP13 |
| A | GLU14 |
| A | GLY15 |
| A | LYS16 |
| A | GLY17 |
| A | HIS41 |
| A | EDO503 |
| A | HOH652 |
| A | HOH825 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | GLY12 |
| A | ASP13 |
| A | GLY40 |
| A | ARG304 |
| A | AMP501 |
| A | MLI502 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | THR128 |
| A | LYS130 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 505 |
| Chain | Residue |
| A | GLU355 |
| A | PRO357 |
| A | ALA358 |
| A | ASN359 |
| B | ASN100 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE AMP B 501 |
| Chain | Residue |
| A | ARG142 |
| B | TRP11 |
| B | ASP13 |
| B | ASN38 |
| B | GLY126 |
| B | THR127 |
| B | THR128 |
| B | GLN223 |
| B | LEU227 |
| B | VAL237 |
| B | THR238 |
| B | VAL272 |
| B | GLY273 |
| B | MLI503 |
| B | FMT508 |
| B | HOH620 |
| B | HOH629 |
| B | HOH632 |
| B | HOH641 |
| B | HOH669 |
| B | HOH672 |
| B | HOH680 |
| B | HOH808 |
| B | HOH869 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MLI B 502 |
| Chain | Residue |
| A | VAL261 |
| A | GLY322 |
| A | THR324 |
| B | GLY254 |
| B | PRO255 |
| B | ALA256 |
| B | LYS257 |
| B | HOH784 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLI B 503 |
| Chain | Residue |
| B | ASN38 |
| B | THR128 |
| B | LYS130 |
| B | AMP501 |
| B | EDO506 |
| B | HOH749 |
| B | HOH769 |
| B | HOH783 |
| B | HOH905 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| A | LYS257 |
| B | ARG318 |
| B | GLY322 |
| B | LEU323 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | GLN198 |
| B | VAL200 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | GLY297 |
| B | THR298 |
| B | THR299 |
| B | THR300 |
| B | MLI503 |
| B | HOH883 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 507 |
| Chain | Residue |
| B | HOH904 |
| B | GLU25 |
| B | HIS26 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT B 508 |
| Chain | Residue |
| B | LYS16 |
| B | ALA39 |
| B | GLY40 |
| B | ALA222 |
| B | GLN223 |
| B | AMP501 |
| B | PO4510 |
| B | HOH869 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 509 |
| Chain | Residue |
| B | GLY126 |
| B | VAL272 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 510 |
| Chain | Residue |
| B | ASP13 |
| B | GLU14 |
| B | GLY15 |
| B | LYS16 |
| B | GLY17 |
| B | GLY40 |
| B | FMT508 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pi.AGgVTVGTG |
| Chain | Residue | Details |
| A | PRO242-GLY252 | |
| site_id | PS00513 |
| Number of Residues | 12 |
| Details | ADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYmdKaaR |
| Chain | Residue | Details |
| A | GLY131-ARG142 | |
| 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 | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00011","evidenceCode":"ECO:0000255"}]} |
