Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0033609 | biological_process | oxalate metabolic process |
A | 0046564 | molecular_function | oxalate decarboxylase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0033609 | biological_process | oxalate metabolic process |
B | 0046564 | molecular_function | oxalate decarboxylase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0033609 | biological_process | oxalate metabolic process |
C | 0046564 | molecular_function | oxalate decarboxylase activity |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue ACT A 401 |
Chain | Residue |
A | MET84 |
A | ARG92 |
A | HIS95 |
A | HIS97 |
A | GLU101 |
A | LEU153 |
A | PHE155 |
A | MN411 |
A | HOH523 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue ACT A 402 |
Chain | Residue |
A | VAL243 |
A | ILE245 |
A | ALA260 |
A | ARG270 |
A | GLU333 |
A | TYR340 |
A | HOH671 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue ACT A 403 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue ACT A 404 |
Chain | Residue |
A | VAL222 |
A | PRO225 |
A | HOH673 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ACT A 405 |
Chain | Residue |
A | GLU117 |
A | PRO135 |
A | SER136 |
A | HOH505 |
A | HOH897 |
C | PRO276 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue ACT A 406 |
Chain | Residue |
A | GLY108 |
A | GLY127 |
A | GLU128 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ACT A 407 |
Chain | Residue |
A | GLN143 |
A | ASN204 |
A | GLN205 |
A | HOH659 |
C | THR355 |
C | PHE356 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue ACT A 408 |
Chain | Residue |
A | TYR104 |
A | ILE106 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | LYS87 |
A | GLU146 |
A | HOH676 |
A | HOH788 |
B | GLY13 |
B | ASP14 |
B | GLY16 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MN A 410 |
Chain | Residue |
A | HIS273 |
A | HIS275 |
A | GLU280 |
A | HIS319 |
A | HOH571 |
A | HOH577 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MN A 411 |
Chain | Residue |
A | HIS95 |
A | HIS97 |
A | GLU101 |
A | HIS140 |
A | ACT401 |
A | HOH523 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue ACT B 401 |
Chain | Residue |
B | MET84 |
B | ARG92 |
B | HIS95 |
B | HIS97 |
B | GLU101 |
B | LEU153 |
B | PHE155 |
B | TYR200 |
B | MN408 |
B | HOH545 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue ACT B 402 |
Chain | Residue |
B | VAL243 |
B | ILE245 |
B | ALA260 |
B | ARG270 |
B | GLU333 |
B | TYR340 |
B | HOH646 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue ACT B 403 |
Chain | Residue |
B | HIS56 |
B | ARG58 |
B | ASN163 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue ACT B 404 |
Chain | Residue |
B | TYR104 |
B | MET105 |
B | ILE106 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
B | ASP41 |
B | HIS42 |
B | GLY43 |
B | HOH509 |
B | HOH631 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue GOL B 406 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue MN B 407 |
Chain | Residue |
B | HIS273 |
B | HIS275 |
B | GLU280 |
B | HIS319 |
B | HOH558 |
B | HOH568 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue MN B 408 |
Chain | Residue |
B | HIS95 |
B | HIS97 |
B | GLU101 |
B | HIS140 |
B | ACT401 |
B | HOH545 |
site_id | AE2 |
Number of Residues | 9 |
Details | binding site for residue ACT C 401 |
Chain | Residue |
C | HIS95 |
C | HIS97 |
C | GLU101 |
C | LEU153 |
C | PHE155 |
C | MN406 |
C | HOH523 |
C | MET84 |
C | ARG92 |
site_id | AE3 |
Number of Residues | 8 |
Details | binding site for residue ACT C 402 |
Chain | Residue |
C | VAL243 |
C | ILE245 |
C | ALA260 |
C | VAL262 |
C | ARG270 |
C | GLU333 |
C | TYR340 |
C | HOH641 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue MPD C 403 |
Chain | Residue |
C | TYR104 |
C | ILE106 |
C | HOH763 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue MPD C 404 |
Chain | Residue |
C | LYS87 |
C | HOH511 |
C | HOH667 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue MN C 405 |
Chain | Residue |
C | HIS273 |
C | HIS275 |
C | GLU280 |
C | HIS319 |
C | HOH585 |
C | HOH586 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue MN C 406 |
Chain | Residue |
C | HIS95 |
C | HIS97 |
C | GLU101 |
C | HIS140 |
C | ACT401 |
C | HOH523 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU333 | |
B | GLU333 | |
C | GLU333 | |
Chain | Residue | Details |
B | HIS273 | |
B | HIS275 | |
B | GLU280 | |
B | HIS319 | |
C | HIS95 | |
C | HIS97 | |
C | GLU101 | |
C | HIS140 | |
C | HIS273 | |
C | HIS275 | |
C | GLU280 | |
C | HIS319 | |
A | HIS95 | |
A | HIS97 | |
A | GLU101 | |
A | HIS140 | |
A | HIS273 | |
A | HIS275 | |
A | GLU280 | |
A | HIS319 | |
B | HIS95 | |
B | HIS97 | |
B | GLU101 | |
B | HIS140 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 231 |
Chain | Residue | Details |
A | ARG92 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
A | HIS95 | metal ligand |
A | HIS97 | metal ligand |
A | GLU101 | metal ligand |
A | HIS140 | metal ligand |
A | GLU162 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 231 |
Chain | Residue | Details |
B | ARG92 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
B | HIS95 | metal ligand |
B | HIS97 | metal ligand |
B | GLU101 | metal ligand |
B | HIS140 | metal ligand |
B | GLU162 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 231 |
Chain | Residue | Details |
C | ARG92 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
C | HIS95 | metal ligand |
C | HIS97 | metal ligand |
C | GLU101 | metal ligand |
C | HIS140 | metal ligand |
C | GLU162 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |