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 |