3D03
1.9A structure of Glycerophoshphodiesterase (GpdQ) from Enterobacter aerogenes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| A | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| A | 0006071 | biological_process | glycerol metabolic process |
| A | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| B | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| B | 0006071 | biological_process | glycerol metabolic process |
| B | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| C | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| C | 0006071 | biological_process | glycerol metabolic process |
| C | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| D | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| D | 0006071 | biological_process | glycerol metabolic process |
| D | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| E | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| E | 0006071 | biological_process | glycerol metabolic process |
| E | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| F | 0004115 | molecular_function | 3',5'-cyclic-AMP phosphodiesterase activity |
| F | 0006071 | biological_process | glycerol metabolic process |
| F | 0008889 | molecular_function | glycerophosphodiester phosphodiesterase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 1001 |
| Chain | Residue |
| A | ASP8 |
| A | HIS10 |
| A | ASP50 |
| A | HIS197 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 1002 |
| Chain | Residue |
| A | ASP50 |
| A | ASN80 |
| A | HIS156 |
| A | HIS195 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 1001 |
| Chain | Residue |
| B | HIS10 |
| B | ASP50 |
| B | HIS197 |
| B | ASP8 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 1002 |
| Chain | Residue |
| B | ASP50 |
| B | ASN80 |
| B | HIS156 |
| B | HIS195 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO C 1001 |
| Chain | Residue |
| C | ASP8 |
| C | HIS10 |
| C | ASP50 |
| C | HIS197 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO C 1002 |
| Chain | Residue |
| C | ASP50 |
| C | ASN80 |
| C | HIS156 |
| C | HIS195 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO D 1001 |
| Chain | Residue |
| D | ASP8 |
| D | HIS10 |
| D | ASP50 |
| D | HIS197 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO D 1002 |
| Chain | Residue |
| D | ASP50 |
| D | ASN80 |
| D | HIS156 |
| D | HIS195 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO E 1001 |
| Chain | Residue |
| E | ASP8 |
| E | HIS10 |
| E | ASP50 |
| E | HIS197 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO E 1002 |
| Chain | Residue |
| E | ASP50 |
| E | ASN80 |
| E | HIS156 |
| E | HIS195 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO F 1001 |
| Chain | Residue |
| F | ASP8 |
| F | HIS10 |
| F | ASP50 |
| F | HIS197 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO F 1002 |
| Chain | Residue |
| F | ASP50 |
| F | ASN80 |
| F | HIS156 |
| F | HIS195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18678932, ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553, ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA |
| Chain | Residue | Details |
| A | ASP8 | |
| B | ASP50 | |
| B | ASN80 | |
| B | HIS156 | |
| B | HIS195 | |
| B | HIS197 | |
| C | ASP8 | |
| C | HIS10 | |
| C | ASP50 | |
| C | ASN80 | |
| C | HIS156 | |
| A | HIS10 | |
| C | HIS195 | |
| C | HIS197 | |
| D | ASP8 | |
| D | HIS10 | |
| D | ASP50 | |
| D | ASN80 | |
| D | HIS156 | |
| D | HIS195 | |
| D | HIS197 | |
| E | ASP8 | |
| A | ASP50 | |
| E | HIS10 | |
| E | ASP50 | |
| E | ASN80 | |
| E | HIS156 | |
| E | HIS195 | |
| E | HIS197 | |
| F | ASP8 | |
| F | HIS10 | |
| F | ASP50 | |
| F | ASN80 | |
| A | ASN80 | |
| F | HIS156 | |
| F | HIS195 | |
| F | HIS197 | |
| A | HIS156 | |
| A | HIS195 | |
| A | HIS197 | |
| B | ASP8 | |
| B | HIS10 |
