2DVT
Crystal Structure of 2,6-Dihydroxybenzoate Decarboxylase from Rhizobium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019748 | biological_process | secondary metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019748 | biological_process | secondary metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019748 | biological_process | secondary metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019748 | biological_process | secondary metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1501 |
| Chain | Residue |
| A | GLU8 |
| A | HIS10 |
| A | HIS164 |
| A | ASP287 |
| A | HOH1529 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1502 |
| Chain | Residue |
| B | HOH1541 |
| B | GLU8 |
| B | HIS10 |
| B | HIS164 |
| B | ASP287 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 1503 |
| Chain | Residue |
| C | GLU8 |
| C | HIS10 |
| C | HIS164 |
| C | ASP287 |
| C | HOH1555 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 1504 |
| Chain | Residue |
| D | GLU8 |
| D | HIS10 |
| D | HIS164 |
| D | ASP287 |
| D | HOH1550 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:16963440 |
| Chain | Residue | Details |
| A | ASP287 | |
| B | ASP287 | |
| C | ASP287 | |
| D | ASP287 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16963440, ECO:0007744|PDB:2DVT, ECO:0007744|PDB:2DVU, ECO:0007744|PDB:2DVX |
| Chain | Residue | Details |
| A | GLU8 | |
| C | HIS10 | |
| C | HIS164 | |
| C | ASP287 | |
| D | GLU8 | |
| D | HIS10 | |
| D | HIS164 | |
| D | ASP287 | |
| A | HIS10 | |
| A | HIS164 | |
| A | ASP287 | |
| B | GLU8 | |
| B | HIS10 | |
| B | HIS164 | |
| B | ASP287 | |
| C | GLU8 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16963440, ECO:0007744|PDB:2DVU |
| Chain | Residue | Details |
| A | PHE23 | |
| B | PHE23 | |
| C | PHE23 | |
| D | PHE23 |
