Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004055 | molecular_function | argininosuccinate synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| B | 0004055 | molecular_function | argininosuccinate synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| C | 0004055 | molecular_function | argininosuccinate synthase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006526 | biological_process | arginine biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| D | 0004055 | molecular_function | argininosuccinate synthase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006526 | biological_process | arginine biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ANP A 510 |
| Chain | Residue |
| A | ALA6 |
| A | GLN37 |
| A | HIS113 |
| A | GLY114 |
| A | ARG520 |
| A | HOH4314 |
| A | HOH4783 |
| A | SER8 |
| A | GLY10 |
| A | LEU11 |
| A | ASP12 |
| A | THR13 |
| A | PHE31 |
| A | THR32 |
| A | ALA33 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ANP B 1510 |
| Chain | Residue |
| B | ALA6 |
| B | TYR7 |
| B | SER8 |
| B | GLY10 |
| B | LEU11 |
| B | ASP12 |
| B | THR13 |
| B | PHE31 |
| B | THR32 |
| B | ALA33 |
| B | GLN37 |
| B | ARG92 |
| B | HIS113 |
| B | GLY114 |
| B | PHE125 |
| B | ARG1520 |
| B | HOH4252 |
| B | HOH4699 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ANP C 2510 |
| Chain | Residue |
| C | ALA6 |
| C | SER8 |
| C | GLY10 |
| C | LEU11 |
| C | ASP12 |
| C | THR13 |
| C | PHE31 |
| C | THR32 |
| C | ALA33 |
| C | GLN37 |
| C | ARG92 |
| C | HIS113 |
| C | GLY114 |
| C | PHE125 |
| C | ARG2520 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP D 3510 |
| Chain | Residue |
| D | ALA6 |
| D | TYR7 |
| D | SER8 |
| D | GLY10 |
| D | LEU11 |
| D | ASP12 |
| D | THR13 |
| D | PHE31 |
| D | THR32 |
| D | ALA33 |
| D | GLN37 |
| D | ARG92 |
| D | HIS113 |
| D | GLY114 |
| D | PHE125 |
| D | ARG3520 |
| D | HOH4319 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ARG A 520 |
| Chain | Residue |
| A | TYR84 |
| A | THR88 |
| A | SER89 |
| A | ARG92 |
| A | ASN120 |
| A | ASP121 |
| A | ARG124 |
| A | SER173 |
| A | GLU184 |
| A | GLU258 |
| A | TYR270 |
| A | TYR310 |
| A | ANP510 |
| A | SIN530 |
| A | HOH4018 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ARG B 1520 |
| Chain | Residue |
| B | TYR84 |
| B | SER89 |
| B | ARG92 |
| B | ASN120 |
| B | ASP121 |
| B | ARG124 |
| B | GLU184 |
| B | GLU258 |
| B | TYR270 |
| B | TYR310 |
| B | ANP1510 |
| B | SIN1530 |
| B | HOH4065 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG C 2520 |
| Chain | Residue |
| C | SER173 |
| C | GLU184 |
| C | GLU258 |
| C | TYR270 |
| C | TYR310 |
| C | ANP2510 |
| C | SIN2530 |
| C | HOH4172 |
| C | TYR84 |
| C | SER89 |
| C | ARG92 |
| C | ASN120 |
| C | ASP121 |
| C | ARG124 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ARG D 3520 |
| Chain | Residue |
| D | TYR84 |
| D | SER89 |
| D | ARG92 |
| D | ASN120 |
| D | ASP121 |
| D | ARG124 |
| D | SER173 |
| D | SER182 |
| D | GLU184 |
| D | GLU258 |
| D | TYR270 |
| D | TYR310 |
| D | ANP3510 |
| D | SIN3530 |
| D | HOH4261 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SIN A 530 |
| Chain | Residue |
| A | ALA115 |
| A | THR116 |
| A | GLY119 |
| A | ASN120 |
| A | ASP121 |
| A | ARG520 |
| A | HOH4018 |
| A | HOH4226 |
| A | HOH4248 |
| A | HOH4783 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SIN B 1530 |
| Chain | Residue |
| B | ALA115 |
| B | THR116 |
| B | GLY119 |
| B | ASN120 |
| B | ASP121 |
| B | ARG1520 |
| B | HOH4065 |
| B | HOH4265 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SIN C 2530 |
| Chain | Residue |
| C | ALA115 |
| C | THR116 |
| C | GLY119 |
| C | ASN120 |
| C | ASP121 |
| C | GLU184 |
| C | ARG2520 |
| C | HOH4098 |
| C | HOH4172 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SIN D 3530 |
| Chain | Residue |
| D | ALA115 |
| D | THR116 |
| D | GLY119 |
| D | ASN120 |
| D | ASP121 |
| D | GLU184 |
| D | ARG3520 |
| D | HOH4164 |
| D | HOH4261 |
Functional Information from PROSITE/UniProt
| site_id | PS00564 |
| Number of Residues | 9 |
| Details | ARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS |
| Chain | Residue | Details |
| A | ALA6-SER14 | |
| site_id | PS00565 |
| Number of Residues | 12 |
| Details | ARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF |
| Chain | Residue | Details |
| A | GLY114-PHE125 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ALA6 | |
| D | ALA6 | |
| D | ALA33 | |
| D | GLY114 | |
| A | ALA33 | |
| A | GLY114 | |
| B | ALA6 | |
| B | ALA33 | |
| B | GLY114 | |
| C | ALA6 | |
| C | ALA33 | |
| C | GLY114 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR84 | |
| A | TYR270 | |
| B | TYR84 | |
| B | SER89 | |
| B | THR116 | |
| B | ASN120 | |
| B | ASP121 | |
| B | ARG124 | |
| B | SER173 | |
| B | SER182 | |
| B | GLU258 | |
| A | SER89 | |
| B | TYR270 | |
| C | TYR84 | |
| C | SER89 | |
| C | THR116 | |
| C | ASN120 | |
| C | ASP121 | |
| C | ARG124 | |
| C | SER173 | |
| C | SER182 | |
| C | GLU258 | |
| A | THR116 | |
| C | TYR270 | |
| D | TYR84 | |
| D | SER89 | |
| D | THR116 | |
| D | ASN120 | |
| D | ASP121 | |
| D | ARG124 | |
| D | SER173 | |
| D | SER182 | |
| D | GLU258 | |
| A | ASN120 | |
| D | TYR270 | |
| A | ASP121 | |
| A | ARG124 | |
| A | SER173 | |
| A | SER182 | |
| A | GLU258 | |
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 |
