4B2O
Crystal structure of Bacillus subtilis YmdB, a global regulator of late adaptive responses.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008663 | molecular_function | 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008663 | molecular_function | 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008663 | molecular_function | 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008663 | molecular_function | 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1265 |
| Chain | Residue |
| A | GLU39 |
| A | HOH2422 |
| A | HOH2423 |
| A | ASN40 |
| A | ASN67 |
| A | HIS68 |
| A | HIS175 |
| A | HIS177 |
| A | FE21266 |
| A | FE21267 |
| A | HOH2010 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 1266 |
| Chain | Residue |
| A | ASP8 |
| A | GLU39 |
| A | ASN40 |
| A | HIS177 |
| A | PO41265 |
| A | FE21267 |
| A | HOH2010 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 1267 |
| Chain | Residue |
| A | GLU39 |
| A | ASN67 |
| A | HIS150 |
| A | HIS175 |
| A | PO41265 |
| A | FE21266 |
| A | HOH2010 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1265 |
| Chain | Residue |
| B | GLU39 |
| B | ASN40 |
| B | ASN67 |
| B | HIS68 |
| B | HIS175 |
| B | HIS177 |
| B | FE21266 |
| B | FE21267 |
| B | HOH2008 |
| B | HOH2135 |
| B | HOH2262 |
| B | HOH2267 |
| B | HOH2362 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 B 1266 |
| Chain | Residue |
| B | ASP8 |
| B | GLU39 |
| B | ASN40 |
| B | HIS177 |
| B | PO41265 |
| B | FE21267 |
| B | HOH2008 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 B 1267 |
| Chain | Residue |
| B | GLU39 |
| B | ASN67 |
| B | HIS150 |
| B | HIS175 |
| B | PO41265 |
| B | FE21266 |
| B | HOH2008 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 C 1265 |
| Chain | Residue |
| C | GLU39 |
| C | ASN40 |
| C | ASN67 |
| C | HIS68 |
| C | HIS175 |
| C | HIS177 |
| C | FE21266 |
| C | FE21267 |
| C | HOH2008 |
| C | HOH2245 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 C 1266 |
| Chain | Residue |
| C | GLU39 |
| C | ASN67 |
| C | HIS150 |
| C | HIS175 |
| C | PO41265 |
| C | FE21267 |
| C | HOH2008 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 C 1267 |
| Chain | Residue |
| C | ASP8 |
| C | GLU39 |
| C | ASN40 |
| C | HIS177 |
| C | PO41265 |
| C | FE21266 |
| C | HOH2008 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 D 1265 |
| Chain | Residue |
| D | GLU39 |
| D | ASN40 |
| D | ASN67 |
| D | HIS68 |
| D | HIS175 |
| D | HIS177 |
| D | FE21266 |
| D | FE21267 |
| D | HOH2005 |
| D | HOH2097 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 D 1266 |
| Chain | Residue |
| D | GLU39 |
| D | ASN67 |
| D | HIS150 |
| D | HIS175 |
| D | PO41265 |
| D | FE21267 |
| D | HOH2005 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 D 1267 |
| Chain | Residue |
| D | HOH2005 |
| D | ASP8 |
| D | GLU39 |
| D | ASN40 |
| D | HIS177 |
| D | PO41265 |
| D | FE21266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24163345 |
| Chain | Residue | Details |
| A | HIS68 | |
| B | HIS68 | |
| C | HIS68 | |
| D | HIS68 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24163345, ECO:0007744|PDB:4B2O |
| Chain | Residue | Details |
| B | GLU39 | |
| B | ASN40 | |
| B | ASN67 | |
| B | HIS150 | |
| B | HIS175 | |
| B | HIS177 | |
| C | ASP8 | |
| C | GLU39 | |
| C | ASN40 | |
| C | ASN67 | |
| C | HIS150 | |
| C | HIS175 | |
| C | HIS177 | |
| D | ASP8 | |
| D | GLU39 | |
| D | ASN40 | |
| D | ASN67 | |
| D | HIS150 | |
| D | HIS175 | |
| D | HIS177 | |
| A | ASP8 | |
| A | GLU39 | |
| A | ASN40 | |
| A | ASN67 | |
| A | HIS150 | |
| A | HIS175 | |
| A | HIS177 | |
| B | ASP8 |
