6PA5
ECAII(T89V,K162T) MUTANT IN COMPLEX WITH L-ASN AT PH 8.3 IN SPACE GROUP P2(1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| 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 | 0006520 | biological_process | amino acid metabolic process |
| 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 | 0006520 | biological_process | amino acid metabolic process |
| 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 | 0006520 | biological_process | amino acid metabolic process |
| 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 |
| E | 0004067 | molecular_function | asparaginase activity |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006528 | biological_process | asparagine metabolic process |
| E | 0006530 | biological_process | asparagine catabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0051289 | biological_process | protein homotetramerization |
| F | 0004067 | molecular_function | asparaginase activity |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006528 | biological_process | asparagine metabolic process |
| F | 0006530 | biological_process | asparagine catabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| F | 0032991 | cellular_component | protein-containing complex |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0051289 | biological_process | protein homotetramerization |
| G | 0004067 | molecular_function | asparaginase activity |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0006528 | biological_process | asparagine metabolic process |
| G | 0006530 | biological_process | asparagine catabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| G | 0032991 | cellular_component | protein-containing complex |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0051289 | biological_process | protein homotetramerization |
| H | 0004067 | molecular_function | asparaginase activity |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0006528 | biological_process | asparagine metabolic process |
| H | 0006530 | biological_process | asparagine catabolic process |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| H | 0032991 | cellular_component | protein-containing complex |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue ASN A 401 |
| Chain | Residue |
| A | GLY11 |
| A | ALA114 |
| A | HOH548 |
| A | HOH651 |
| C | ASN248 |
| C | GLU283 |
| A | THR12 |
| A | VAL27 |
| A | GLY57 |
| A | SER58 |
| A | GLN59 |
| A | GLY88 |
| A | VAL89 |
| A | ASP90 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue IMD A 402 |
| Chain | Residue |
| A | ASN3 |
| A | ILE4 |
| A | THR5 |
| A | ASN47 |
| A | LYS49 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | ASP281 |
| A | ALA282 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue ASN B 401 |
| Chain | Residue |
| B | GLY11 |
| B | THR12 |
| B | VAL27 |
| B | GLY57 |
| B | SER58 |
| B | GLN59 |
| B | GLY88 |
| B | VAL89 |
| B | ASP90 |
| B | ALA114 |
| B | HOH519 |
| B | HOH635 |
| D | ASN248 |
| D | GLU283 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 402 |
| Chain | Residue |
| B | ASN3 |
| B | ILE4 |
| B | THR5 |
| B | ASN47 |
| B | LYS49 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | ASP281 |
| B | ALA282 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue ASN C 401 |
| Chain | Residue |
| A | ASN248 |
| A | GLU283 |
| C | GLY11 |
| C | THR12 |
| C | GLY57 |
| C | SER58 |
| C | GLN59 |
| C | GLY88 |
| C | VAL89 |
| C | ASP90 |
| C | ALA114 |
| C | HOH642 |
| C | HOH656 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue IMD C 402 |
| Chain | Residue |
| C | ASN3 |
| C | ILE4 |
| C | THR5 |
| C | ASN47 |
| C | LYS49 |
| C | LYS79 |
| C | THR80 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue ASN D 401 |
| Chain | Residue |
| B | ASN248 |
| B | GLU283 |
| D | GLY11 |
| D | THR12 |
| D | GLY57 |
| D | SER58 |
| D | GLN59 |
| D | GLY88 |
| D | VAL89 |
| D | ASP90 |
| D | ALA114 |
| D | HOH621 |
| D | HOH655 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue IMD D 402 |
| Chain | Residue |
| D | ASN3 |
| D | ILE4 |
| D | THR5 |
| D | ASN47 |
| D | LYS49 |
| D | LYS79 |
| D | THR80 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 403 |
| Chain | Residue |
| A | HOH506 |
| D | SER120 |
| D | MET121 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue ASN E 401 |
| Chain | Residue |
| E | GLY11 |
| E | THR12 |
| E | GLY57 |
| E | SER58 |
| E | GLN59 |
| E | GLY88 |
| E | VAL89 |
| E | ASP90 |
| E | ALA114 |
| E | HOH616 |
| E | HOH617 |
| G | GLU283 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue IMD E 402 |
| Chain | Residue |
| E | ASN47 |
| E | LYS49 |
| E | LYS79 |
| E | THR80 |
| E | HOH676 |
| E | ILE4 |
| E | THR5 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue ASN F 401 |
| Chain | Residue |
| F | GLY11 |
| F | THR12 |
| F | GLY57 |
| F | SER58 |
| F | GLN59 |
| F | GLY88 |
| F | VAL89 |
| F | ASP90 |
| F | ALA114 |
| F | HOH616 |
| F | HOH619 |
| H | GLU283 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue IMD F 402 |
| Chain | Residue |
| F | ILE4 |
| F | THR5 |
| F | ASN47 |
| F | LYS49 |
| F | THR80 |
| F | HOH678 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue ASN G 401 |
| Chain | Residue |
| E | ASN248 |
| E | GLU283 |
| G | GLY11 |
| G | THR12 |
| G | GLY57 |
| G | SER58 |
| G | GLN59 |
| G | GLY88 |
| G | VAL89 |
| G | ASP90 |
| G | ALA114 |
| G | HOH646 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue IMD G 402 |
| Chain | Residue |
| G | ASN3 |
| G | ILE4 |
| G | THR5 |
| G | ASN47 |
| G | LYS49 |
| site_id | AD9 |
| Number of Residues | 12 |
| Details | binding site for residue ASN H 401 |
| Chain | Residue |
| F | ASN248 |
| F | GLU283 |
| H | GLY11 |
| H | THR12 |
| H | GLY57 |
| H | SER58 |
| H | GLN59 |
| H | GLY88 |
| H | VAL89 |
| H | ASP90 |
| H | ALA114 |
| H | HOH642 |
Functional Information from PROSITE/UniProt
| site_id | PS00144 |
| Number of Residues | 9 |
| Details | ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA |
| Chain | Residue | Details |
| A | ILE6-ALA14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| 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 | THR12 | |
| B | THR12 | |
| C | THR12 | |
| D | THR12 | |
| E | THR12 | |
| F | THR12 | |
| G | THR12 | |
| H | THR12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA |
| Chain | Residue | Details |
| A | SER58 | |
| E | VAL89 | |
| F | SER58 | |
| F | VAL89 | |
| G | SER58 | |
| G | VAL89 | |
| H | SER58 | |
| H | VAL89 | |
| A | VAL89 | |
| B | SER58 | |
| B | VAL89 | |
| C | SER58 | |
| C | VAL89 | |
| D | SER58 | |
| D | VAL89 | |
| E | SER58 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| A | THR12 | 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 | THR12 | 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 | THR12 | 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 | THR12 | 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 |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| E | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| E | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| E | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| E | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| E | THR162 | proton acceptor, proton donor |
| E | GLU283 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| F | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| F | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| F | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| F | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| F | THR162 | proton acceptor, proton donor |
| F | GLU283 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| G | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| G | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| G | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| G | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| G | THR162 | proton acceptor, proton donor |
| G | GLU283 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| H | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| H | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| H | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| H | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| H | THR162 | proton acceptor, proton donor |
| H | GLU283 | electrostatic stabiliser |
