2OGI
Crystal structure of a putative metal dependent phosphohydrolase (sag1661) from streptococcus agalactiae serogroup v at 1.85 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008803 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008803 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (symmetrical) 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 | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 301 |
| Chain | Residue |
| A | HIS29 |
| A | HIS58 |
| A | ASP59 |
| A | ASP135 |
| A | FE302 |
| A | GDP400 |
| A | HOH406 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 302 |
| Chain | Residue |
| A | HIS117 |
| A | FE301 |
| A | GDP400 |
| A | HOH406 |
| A | ASP59 |
| A | HIS91 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 301 |
| Chain | Residue |
| B | HIS29 |
| B | HIS58 |
| B | ASP59 |
| B | ASP135 |
| B | FE302 |
| B | GDP400 |
| B | HOH413 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 302 |
| Chain | Residue |
| B | ASP59 |
| B | HIS91 |
| B | HIS117 |
| B | FE301 |
| B | GDP400 |
| B | HOH413 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 303 |
| Chain | Residue |
| A | GLY145 |
| A | VAL146 |
| A | GLU147 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 305 |
| Chain | Residue |
| A | ARG35 |
| A | HIS139 |
| A | HOH445 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDP A 400 |
| Chain | Residue |
| A | HIS29 |
| A | ASP59 |
| A | LYS62 |
| A | ASN88 |
| A | HIS91 |
| A | HIS117 |
| A | THR118 |
| A | ASP135 |
| A | ARG141 |
| A | LEU172 |
| A | PRO178 |
| A | ILE179 |
| A | TYR180 |
| A | THR183 |
| A | FE301 |
| A | FE302 |
| A | HOH406 |
| A | HOH412 |
| A | HOH414 |
| A | HOH444 |
| A | HOH462 |
| A | HOH515 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDP B 400 |
| Chain | Residue |
| B | HIS29 |
| B | ASP59 |
| B | LYS62 |
| B | ASN88 |
| B | HIS91 |
| B | HIS117 |
| B | THR118 |
| B | ASP135 |
| B | ARG141 |
| B | THR168 |
| B | LEU172 |
| B | PRO178 |
| B | TYR180 |
| B | THR183 |
| B | FE301 |
| B | FE302 |
| B | HOH413 |
| B | HOH421 |
| B | HOH422 |
| B | HOH442 |
| B | HOH465 |
| B | HOH467 |
| B | HOH494 |
| B | HOH506 |
| B | HOH523 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 401 |
| Chain | Residue |
| B | THR2 |
| B | TYR3 |
| B | ARG11 |
| B | ILE38 |
| B | LYS48 |
| B | GLU49 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2OGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of conserved hypothetical protein TIGR00488 (NP_688652.1) from Streptococcus agalactiae 2603 at 1.85 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
