2PZ0
Crystal structure of Glycerophosphodiester Phosphodiesterase (GDPD) from T. tengcongensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0006629 | biological_process | lipid metabolic process |
B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 501 |
Chain | Residue |
A | GLU44 |
A | ASP46 |
A | GLU119 |
A | HOH503 |
A | HOH628 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 502 |
Chain | Residue |
B | HOH607 |
B | GLU44 |
B | ASP46 |
B | GLU119 |
B | HOH503 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 400 |
Chain | Residue |
B | HIS17 |
B | GLU44 |
B | GLU119 |
B | PHE152 |
B | LEU172 |
B | HOH504 |
B | HOH538 |
B | HOH607 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 401 |
Chain | Residue |
A | HIS17 |
A | GLU44 |
A | GLU119 |
A | PHE152 |
A | LEU172 |
A | TRP217 |
A | HOH503 |
A | HOH505 |
A | HOH521 |
A | HOH527 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:18214974, ECO:0007744|PDB:2PZ0 |
Chain | Residue | Details |
A | HIS17 | |
B | HIS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:18214974, ECO:0007744|PDB:2PZ0 |
Chain | Residue | Details |
A | HIS59 | |
B | HIS59 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18214974, ECO:0007744|PDB:2PZ0 |
Chain | Residue | Details |
A | GLU44 | |
A | ASP46 | |
A | GLU119 | |
B | GLU44 | |
B | ASP46 | |
B | GLU119 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 300 |
Chain | Residue | Details |
A | HIS17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG18 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | GLU44 | metal ligand |
A | ASP46 | metal ligand |
A | HIS59 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU119 | metal ligand |
A | LYS121 | electrostatic stabiliser, hydrogen bond donor |
A | ASP239 | hydrogen bond acceptor, increase acidity, increase basicity |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 300 |
Chain | Residue | Details |
B | HIS17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG18 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | GLU44 | metal ligand |
B | ASP46 | metal ligand |
B | HIS59 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLU119 | metal ligand |
B | LYS121 | electrostatic stabiliser, hydrogen bond donor |
B | ASP239 | hydrogen bond acceptor, increase acidity, increase basicity |