1KH1
Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000050 | biological_process | urea cycle |
A | 0000053 | biological_process | argininosuccinate metabolic process |
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 | 0000050 | biological_process | urea cycle |
B | 0000053 | biological_process | argininosuccinate metabolic process |
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 | 0000050 | biological_process | urea cycle |
C | 0000053 | biological_process | argininosuccinate metabolic process |
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 | 0000050 | biological_process | urea cycle |
D | 0000053 | biological_process | argininosuccinate metabolic process |
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 510 |
Chain | Residue |
A | SER8 |
A | GLY10 |
A | ASP12 |
A | THR13 |
A | HOH1457 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1510 |
Chain | Residue |
B | HOH1194 |
B | HOH1226 |
B | SER8 |
B | GLY10 |
B | ASP12 |
B | THR13 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 2510 |
Chain | Residue |
C | SER8 |
C | GLY10 |
C | ASP12 |
C | THR13 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 3510 |
Chain | Residue |
D | SER8 |
D | GLY10 |
D | ASP12 |
D | THR13 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518 |
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 |