1KOR
Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with inhibitors
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 | 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
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 |