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 | 16 |
Details | BINDING SITE FOR RESIDUE ATP A 510 |
Chain | Residue |
A | ALA6 |
A | HIS113 |
A | GLY114 |
A | PHE125 |
A | SER173 |
A | ASP175 |
A | CIR520 |
A | ASP530 |
A | SER8 |
A | ASP12 |
A | THR13 |
A | PHE31 |
A | THR32 |
A | ALA33 |
A | GLN37 |
A | ARG92 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ATP B 2510 |
Chain | Residue |
A | ASP2530 |
B | ALA6 |
B | TYR7 |
B | SER8 |
B | GLY10 |
B | ASP12 |
B | THR13 |
B | PHE31 |
B | THR32 |
B | ALA33 |
B | GLN37 |
B | ARG92 |
B | HIS113 |
B | GLY114 |
B | PHE125 |
B | HOH1506 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP C 3510 |
Chain | Residue |
A | ASP3530 |
C | ALA6 |
C | SER8 |
C | ASP12 |
C | THR13 |
C | PHE31 |
C | THR32 |
C | ALA33 |
C | GLN37 |
C | ARG92 |
C | ILE95 |
C | HIS113 |
C | GLY114 |
C | ALA115 |
C | PHE125 |
C | SER173 |
C | ASP175 |
C | HOH1541 |
C | CIR3520 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ATP D 4510 |
Chain | Residue |
A | ASP4530 |
D | ALA6 |
D | TYR7 |
D | SER8 |
D | GLY10 |
D | LEU11 |
D | ASP12 |
D | THR13 |
D | PHE31 |
D | ALA33 |
D | GLN37 |
D | ARG92 |
D | HIS113 |
D | GLY114 |
D | PHE125 |
D | HOH1479 |
D | CIR4520 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIR A 520 |
Chain | Residue |
A | TYR84 |
A | THR88 |
A | SER89 |
A | ASN120 |
A | ARG124 |
A | SER173 |
A | MET174 |
A | SER182 |
A | GLU184 |
A | GLU258 |
A | TYR270 |
A | TYR310 |
A | ATP510 |
A | ASP530 |
A | HOH1017 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIR B 2520 |
Chain | Residue |
A | ASP2530 |
B | TYR84 |
B | THR88 |
B | SER89 |
B | ASN120 |
B | ARG124 |
B | SER173 |
B | MET174 |
B | ASP175 |
B | SER182 |
B | GLU184 |
B | GLU258 |
B | TYR270 |
B | TYR310 |
B | HOH1039 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIR C 3520 |
Chain | Residue |
C | TYR84 |
C | THR88 |
C | SER89 |
C | ASN120 |
C | ASP121 |
C | ARG124 |
C | SER173 |
C | MET174 |
C | SER182 |
C | GLU184 |
C | GLU258 |
C | TYR270 |
C | TYR310 |
C | ATP3510 |
A | ASP3530 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CIR D 4520 |
Chain | Residue |
A | HOH1124 |
A | ASP4530 |
D | TYR84 |
D | THR88 |
D | SER89 |
D | ASN120 |
D | ARG124 |
D | SER173 |
D | MET174 |
D | ASP175 |
D | SER182 |
D | GLU184 |
D | GLU258 |
D | TYR270 |
D | TYR310 |
D | ATP4510 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASP A 530 |
Chain | Residue |
A | ALA115 |
A | THR116 |
A | GLY119 |
A | ASN120 |
A | ASP121 |
A | ATP510 |
A | CIR520 |
A | HOH1017 |
A | HOH1071 |
A | HOH1159 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASP A 2530 |
Chain | Residue |
A | HOH1049 |
B | ALA115 |
B | THR116 |
B | GLY119 |
B | ASN120 |
B | ASP121 |
B | HOH1039 |
B | HOH1099 |
B | ATP2510 |
B | CIR2520 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASP A 3530 |
Chain | Residue |
A | HOH1004 |
A | HOH1117 |
C | ALA115 |
C | THR116 |
C | GLY119 |
C | ASN120 |
C | ASP121 |
C | HOH1028 |
C | ATP3510 |
C | CIR3520 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ASP A 4530 |
Chain | Residue |
A | HOH1124 |
A | HOH1161 |
D | ALA115 |
D | THR116 |
D | GLY119 |
D | ASN120 |
D | ASP121 |
D | GLU184 |
D | HOH1212 |
D | ATP4510 |
D | CIR4520 |
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 |