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3D03

1.9A structure of Glycerophoshphodiesterase (GpdQ) from Enterobacter aerogenes

Functional Information from GO Data
ChainGOidnamespacecontents
A0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
A0006071biological_processglycerol metabolic process
A0008889molecular_functionglycerophosphodiester phosphodiesterase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
B0006071biological_processglycerol metabolic process
B0008889molecular_functionglycerophosphodiester phosphodiesterase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
C0006071biological_processglycerol metabolic process
C0008889molecular_functionglycerophosphodiester phosphodiesterase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
D0006071biological_processglycerol metabolic process
D0008889molecular_functionglycerophosphodiester phosphodiesterase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
E0006071biological_processglycerol metabolic process
E0008889molecular_functionglycerophosphodiester phosphodiesterase activity
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
F0004112molecular_functioncyclic-nucleotide phosphodiesterase activity
F0006071biological_processglycerol metabolic process
F0008889molecular_functionglycerophosphodiester phosphodiesterase activity
F0016787molecular_functionhydrolase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 1001
ChainResidue
AASP8
AHIS10
AASP50
AHIS197

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 1002
ChainResidue
AASP50
AASN80
AHIS156
AHIS195

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 1001
ChainResidue
BHIS10
BASP50
BHIS197
BASP8

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 1002
ChainResidue
BASP50
BASN80
BHIS156
BHIS195

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO C 1001
ChainResidue
CASP8
CHIS10
CASP50
CHIS197

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO C 1002
ChainResidue
CASP50
CASN80
CHIS156
CHIS195

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO D 1001
ChainResidue
DASP8
DHIS10
DASP50
DHIS197

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO D 1002
ChainResidue
DASP50
DASN80
DHIS156
DHIS195

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO E 1001
ChainResidue
EASP8
EHIS10
EASP50
EHIS197

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO E 1002
ChainResidue
EASP50
EASN80
EHIS156
EHIS195

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO F 1001
ChainResidue
FASP8
FHIS10
FASP50
FHIS197

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO F 1002
ChainResidue
FASP50
FASN80
FHIS156
FHIS195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18678932","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17306828","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18831553","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZOA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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