2HIM
Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004067 | molecular_function | asparaginase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0033345 | biological_process | asparagine catabolic process via L-aspartate |
A | 0042802 | molecular_function | identical protein binding |
A | 0051289 | biological_process | protein homotetramerization |
B | 0004067 | molecular_function | asparaginase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0033345 | biological_process | asparagine catabolic process via L-aspartate |
B | 0042802 | molecular_function | identical protein binding |
B | 0051289 | biological_process | protein homotetramerization |
C | 0004067 | molecular_function | asparaginase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0033345 | biological_process | asparagine catabolic process via L-aspartate |
C | 0042802 | molecular_function | identical protein binding |
C | 0051289 | biological_process | protein homotetramerization |
D | 0004067 | molecular_function | asparaginase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0033345 | biological_process | asparagine catabolic process via L-aspartate |
D | 0042802 | molecular_function | identical protein binding |
D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ASP A 7001 |
Chain | Residue |
A | GLY13 |
A | THR14 |
A | ASP59 |
A | SER60 |
A | GLY90 |
A | THR91 |
A | ASP92 |
A | SER117 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ASP B 7002 |
Chain | Residue |
B | THR14 |
B | ASP59 |
B | SER60 |
B | GLY90 |
B | THR91 |
B | ASP92 |
B | SER117 |
B | GLY13 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ASP C 7003 |
Chain | Residue |
A | ASN246 |
C | GLY13 |
C | THR14 |
C | ASP59 |
C | SER60 |
C | GLY90 |
C | THR91 |
C | ASP92 |
C | SER117 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ASP D 7004 |
Chain | Residue |
D | GLY13 |
D | THR14 |
D | ASP59 |
D | SER60 |
D | GLY90 |
D | THR91 |
D | ASP92 |
D | SER117 |
D | HOH5032 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ASN A 8001 |
Chain | Residue |
A | ALA162 |
A | ARG240 |
A | THR271 |
A | GLN272 |
A | CYS273 |
A | THR301 |
A | VAL302 |
A | GLU303 |
A | HOH5249 |
A | EDO9002 |
C | ARG240 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ASN B 8002 |
Chain | Residue |
B | ALA162 |
B | ARG240 |
B | THR271 |
B | GLN272 |
B | CYS273 |
B | THR301 |
B | VAL302 |
B | GLU303 |
B | HOH5398 |
B | EDO9004 |
D | ARG240 |
D | HOH5101 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ASN C 8003 |
Chain | Residue |
A | ARG240 |
C | ALA162 |
C | ARG240 |
C | THR271 |
C | GLN272 |
C | CYS273 |
C | MET274 |
C | THR301 |
C | VAL302 |
C | GLU303 |
C | HOH5220 |
C | EDO9001 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ASN D 8004 |
Chain | Residue |
B | ARG240 |
D | ALA162 |
D | ARG240 |
D | THR271 |
D | GLN272 |
D | CYS273 |
D | THR301 |
D | VAL302 |
D | GLU303 |
D | HOH5151 |
D | HOH5389 |
D | EDO9003 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ASN A 6001 |
Chain | Residue |
A | GLY13 |
A | THR14 |
A | ASP59 |
A | SER60 |
A | SER61 |
A | GLY90 |
A | THR91 |
A | ASP92 |
C | ASN246 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASN B 6002 |
Chain | Residue |
D | ASN246 |
B | GLY13 |
B | THR14 |
B | MET17 |
B | ASP59 |
B | SER60 |
B | SER61 |
B | GLY90 |
B | THR91 |
B | ASP92 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ASN C 6003 |
Chain | Residue |
A | ASN246 |
C | GLY13 |
C | THR14 |
C | MET17 |
C | ASP59 |
C | SER60 |
C | SER61 |
C | GLY90 |
C | THR91 |
C | ASP92 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ASN D 6004 |
Chain | Residue |
B | ASN246 |
D | GLY13 |
D | THR14 |
D | ASP59 |
D | SER60 |
D | SER61 |
D | GLY90 |
D | THR91 |
D | ASP92 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO C 9001 |
Chain | Residue |
C | ASN176 |
C | THR271 |
C | CYS273 |
C | MET274 |
C | SER275 |
C | GLY276 |
C | ASP299 |
C | MET300 |
C | THR301 |
C | ASN8003 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A 9002 |
Chain | Residue |
A | ASN176 |
A | THR271 |
A | CYS273 |
A | MET274 |
A | SER275 |
A | GLY276 |
A | ASP299 |
A | MET300 |
A | THR301 |
A | ASN8001 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO D 9003 |
Chain | Residue |
D | ASN176 |
D | THR271 |
D | CYS273 |
D | MET274 |
D | SER275 |
D | GLY276 |
D | ASP299 |
D | MET300 |
D | ASN8004 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 9004 |
Chain | Residue |
B | ASN176 |
B | THR271 |
B | CYS273 |
B | MET274 |
B | SER275 |
B | GLY276 |
B | ASP299 |
B | MET300 |
B | THR301 |
B | ASN8002 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 9005 |
Chain | Residue |
A | ASP92 |
A | LYS163 |
A | ALA166 |
C | GLY243 |
C | VAL244 |
C | ASN246 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 9006 |
Chain | Residue |
A | ILE185 |
B | ASP92 |
B | GLN118 |
B | LYS163 |
B | ALA166 |
D | GLY243 |
D | VAL244 |
D | ASN246 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 9007 |
Chain | Residue |
A | GLY243 |
A | VAL244 |
A | ASN246 |
C | ASP92 |
C | LYS163 |
C | ALA166 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 9008 |
Chain | Residue |
B | GLY243 |
B | VAL244 |
B | ASN246 |
C | ILE185 |
D | ASP92 |
D | GLN118 |
D | LYS163 |
D | ALA166 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745 |
Chain | Residue | Details |
A | THR14 | |
B | THR14 | |
C | THR14 | |
D | THR14 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0007744|PDB:2P2N |
Chain | Residue | Details |
A | ASP59 | |
B | THR271 | |
C | ASP59 | |
C | THR91 | |
C | ALA162 | |
C | ARG240 | |
C | THR271 | |
D | ASP59 | |
D | THR91 | |
D | ALA162 | |
D | ARG240 | |
A | THR91 | |
D | THR271 | |
A | ALA162 | |
A | ARG240 | |
A | THR271 | |
B | ASP59 | |
B | THR91 | |
B | ALA162 | |
B | ARG240 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | ASP92 | |
A | THR14 | |
A | THR91 | |
A | LYS163 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
B | ASP92 | |
B | THR14 | |
B | THR91 | |
B | LYS163 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
C | ASP92 | |
C | THR14 | |
C | THR91 | |
C | LYS163 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
D | ASP92 | |
D | THR14 | |
D | THR91 | |
D | LYS163 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | LEU289 | |
C | THR14 | |
C | THR91 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
D | THR14 | |
D | THR91 | |
B | LEU289 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | THR14 | |
A | THR91 | |
C | LEU289 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
D | LEU289 | |
B | THR14 | |
B | THR91 |