6NXB
ECAII IN COMPLEX WITH CITRATE AT PH 7
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue CIT A 401 |
Chain | Residue |
A | GLY57 |
A | HOH548 |
A | HOH564 |
A | HOH646 |
A | HOH660 |
B | ASN248 |
B | GLU283 |
A | SER58 |
A | GLN59 |
A | GLY88 |
A | THR89 |
A | ASP90 |
A | ALA114 |
A | HOH502 |
A | HOH514 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | LYS213 |
A | TYR236 |
A | HOH501 |
A | HOH527 |
B | SER224 |
B | ASP225 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue CIT B 401 |
Chain | Residue |
A | ASN248 |
A | GLU283 |
B | GLY57 |
B | SER58 |
B | GLN59 |
B | GLY88 |
B | THR89 |
B | ASP90 |
B | ALA114 |
B | HOH509 |
B | HOH538 |
B | HOH553 |
B | HOH598 |
B | HOH665 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue CIT C 401 |
Chain | Residue |
C | GLY57 |
C | SER58 |
C | GLN59 |
C | GLY88 |
C | THR89 |
C | ASP90 |
C | HOH533 |
C | HOH566 |
C | HOH590 |
C | HOH613 |
C | HOH650 |
C | HOH711 |
D | ASN248 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue CIT C 402 |
Chain | Residue |
C | LYS213 |
C | TYR236 |
C | HOH543 |
C | HOH624 |
C | HOH687 |
D | SER224 |
D | HOH537 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue CIT D 401 |
Chain | Residue |
C | ASN248 |
C | GLU283 |
D | GLY57 |
D | SER58 |
D | GLN59 |
D | GLY88 |
D | THR89 |
D | ASP90 |
D | HOH531 |
D | HOH536 |
D | HOH539 |
D | HOH546 |
D | HOH552 |
D | HOH616 |
D | HOH622 |
D | HOH625 |
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:12595697, ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862 |
Chain | Residue | Details |
A | THR12 | |
B | THR12 | |
C | THR12 | |
D | THR12 |
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 | THR89 | |
B | SER58 | |
B | THR89 | |
C | SER58 | |
C | THR89 | |
D | SER58 | |
D | THR89 |
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 | THR89 | 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 | LYS162 | 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 | THR89 | 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 | LYS162 | 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 | THR89 | 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 | LYS162 | 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 | THR89 | 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 | LYS162 | proton acceptor, proton donor |
D | GLU283 | electrostatic stabiliser |