6V28
Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asp
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004067 | molecular_function | asparaginase activity |
A | 0006528 | biological_process | asparagine metabolic process |
A | 0006530 | biological_process | asparagine catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042597 | cellular_component | periplasmic space |
A | 0042802 | molecular_function | identical protein binding |
A | 0051289 | biological_process | protein homotetramerization |
B | 0004067 | molecular_function | asparaginase activity |
B | 0006528 | biological_process | asparagine metabolic process |
B | 0006530 | biological_process | asparagine catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042597 | cellular_component | periplasmic space |
B | 0042802 | molecular_function | identical protein binding |
B | 0051289 | biological_process | protein homotetramerization |
C | 0004067 | molecular_function | asparaginase activity |
C | 0006528 | biological_process | asparagine metabolic process |
C | 0006530 | biological_process | asparagine catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
C | 0032991 | cellular_component | protein-containing complex |
C | 0042597 | cellular_component | periplasmic space |
C | 0042802 | molecular_function | identical protein binding |
C | 0051289 | biological_process | protein homotetramerization |
D | 0004067 | molecular_function | asparaginase activity |
D | 0006528 | biological_process | asparagine metabolic process |
D | 0006530 | biological_process | asparagine catabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
D | 0032991 | cellular_component | protein-containing complex |
D | 0042597 | cellular_component | periplasmic space |
D | 0042802 | molecular_function | identical protein binding |
D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue IMD A 401 |
Chain | Residue |
A | ASN3 |
A | ILE4 |
A | THR5 |
A | ASN47 |
A | LYS49 |
A | LYS79 |
A | THR80 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue GOL B 901 |
Chain | Residue |
B | GLY10 |
B | GLY11 |
B | ALA14 |
B | GLY28 |
B | VAL30 |
B | GLY31 |
B | VAL32 |
B | GLN52 |
B | ASN55 |
B | HOH1042 |
B | ALA8 |
B | THR9 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL C 901 |
Chain | Residue |
C | ASP286 |
C | ALA287 |
C | GLY290 |
C | PHE291 |
C | PRO316 |
C | GLN317 |
C | GLN320 |
C | HOH1012 |
C | HOH1081 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue GOL C 902 |
Chain | Residue |
C | ASN209 |
C | ASN209 |
C | HOH1250 |
C | HOH1250 |
D | PHE254 |
D | PHE254 |
D | ASP255 |
D | ASP255 |
D | TYR289 |
D | TYR289 |
D | HOH670 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue GOL D 401 |
Chain | Residue |
C | SER224 |
C | LEU226 |
D | TYR236 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue GOL D 402 |
Chain | Residue |
D | SER173 |
D | GLY177 |
D | TYR181 |
D | HOH706 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue GOL D 403 |
Chain | Residue |
D | ALA8 |
D | THR9 |
D | GLY10 |
D | GLY11 |
D | ALA14 |
D | VAL30 |
D | GLY31 |
D | VAL32 |
D | GLN52 |
D | ASN55 |
D | HOH524 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL D 404 |
Chain | Residue |
D | PHE291 |
D | GLN317 |
D | GLN320 |
D | HOH513 |
D | HOH661 |
D | HOH749 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue IMD D 405 |
Chain | Residue |
D | ASN3 |
D | ILE4 |
D | THR5 |
D | ASN47 |
D | LYS79 |
D | THR80 |
site_id | AD1 |
Number of Residues | 19 |
Details | binding site for Di-peptide GLY B 11 and AEI B 12 |
Chain | Residue |
A | ASN248 |
A | GLU283 |
B | GLY10 |
B | ILE13 |
B | ALA14 |
B | GLY15 |
B | TYR25 |
B | VAL27 |
B | ILE56 |
B | GLY57 |
B | SER58 |
B | GLN59 |
B | GLY88 |
B | VAL89 |
B | ASP90 |
B | ALA114 |
B | ARG116 |
B | GOL901 |
B | HOH1109 |
site_id | AD2 |
Number of Residues | 19 |
Details | binding site for Di-peptide AEI B 12 and ILE B 13 |
Chain | Residue |
B | GLY88 |
B | VAL89 |
B | ASP90 |
B | ALA114 |
B | ARG116 |
B | SER118 |
B | HOH1004 |
B | HOH1109 |
A | ASN248 |
A | GLU283 |
B | GLY10 |
B | GLY11 |
B | ALA14 |
B | GLY15 |
B | TYR25 |
B | LEU35 |
B | GLY57 |
B | SER58 |
B | GLN59 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for Di-peptide GLY C 11 and AEI C 12 |
Chain | Residue |
C | GLY10 |
C | ILE13 |
C | ALA14 |
C | GLY15 |
C | TYR25 |
C | ILE56 |
C | GLY57 |
C | SER58 |
C | GLN59 |
C | GLY88 |
C | VAL89 |
C | ASP90 |
C | ALA114 |
C | ARG116 |
C | PRO117 |
C | HOH1170 |
D | ASN248 |
D | GLU283 |
site_id | AD4 |
Number of Residues | 19 |
Details | binding site for Di-peptide AEI C 12 and ILE C 13 |
Chain | Residue |
C | GLY10 |
C | GLY11 |
C | ALA14 |
C | GLY15 |
C | TYR25 |
C | LEU35 |
C | GLY57 |
C | SER58 |
C | GLN59 |
C | GLY88 |
C | VAL89 |
C | ASP90 |
C | ALA114 |
C | ARG116 |
C | PRO117 |
C | HOH1163 |
C | HOH1170 |
D | ASN248 |
D | GLU283 |
site_id | AD5 |
Number of Residues | 18 |
Details | binding site for Di-peptide GLY D 11 and AEI D 12 |
Chain | Residue |
C | ASN248 |
C | GLU283 |
D | GLY10 |
D | ILE13 |
D | ALA14 |
D | GLY15 |
D | TYR25 |
D | VAL27 |
D | ILE56 |
D | GLY57 |
D | SER58 |
D | GLN59 |
D | GLY88 |
D | VAL89 |
D | ASP90 |
D | ALA114 |
D | GOL403 |
D | HOH674 |
site_id | AD6 |
Number of Residues | 18 |
Details | binding site for Di-peptide AEI D 12 and ILE D 13 |
Chain | Residue |
C | ASN248 |
C | GLU283 |
D | GLY10 |
D | GLY11 |
D | ALA14 |
D | GLY15 |
D | TYR25 |
D | VAL27 |
D | LEU35 |
D | GLY57 |
D | SER58 |
D | GLN59 |
D | GLY88 |
D | VAL89 |
D | ASP90 |
D | ALA114 |
D | HOH596 |
D | HOH674 |
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:12595697, ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862 |
Chain | Residue | Details |
A | AEI12 | |
B | AEI12 | |
C | AEI12 | |
D | AEI12 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA |
Chain | Residue | Details |
A | SER58 | |
A | VAL89 | |
B | SER58 | |
B | VAL89 | |
C | SER58 | |
C | VAL89 | |
D | SER58 | |
D | VAL89 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 455 |
Chain | Residue | Details |
A | AEI12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
A | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
A | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
A | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
A | THR162 | proton acceptor, proton donor |
A | GLU283 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 455 |
Chain | Residue | Details |
B | AEI12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
B | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
B | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
B | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
B | THR162 | proton acceptor, proton donor |
B | GLU283 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 455 |
Chain | Residue | Details |
C | AEI12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
C | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
C | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
C | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
C | THR162 | proton acceptor, proton donor |
C | GLU283 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 455 |
Chain | Residue | Details |
D | AEI12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
D | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
D | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
D | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
D | THR162 | proton acceptor, proton donor |
D | GLU283 | electrostatic stabiliser |