2O08
CRYSTAL STRUCTURE OF A PUTATIVE HD SUPERFAMILY HYDROLASE (BH1327) FROM BACILLUS HALODURANS AT 1.90 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 400 |
| Chain | Residue |
| A | HIS21 |
| A | HIS50 |
| A | ASP51 |
| A | ASP127 |
| A | FE401 |
| A | PO4500 |
| A | HOH622 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | HIS109 |
| A | FE400 |
| A | PO4500 |
| A | HOH507 |
| A | HOH622 |
| A | ASP51 |
| A | HIS83 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 A 500 |
| Chain | Residue |
| A | ARG18 |
| A | HIS21 |
| A | ASP51 |
| A | LYS54 |
| A | HIS83 |
| A | ASP127 |
| A | ARG133 |
| A | FE400 |
| A | FE401 |
| A | UNL501 |
| A | HOH622 |
| A | HOH661 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 400 |
| Chain | Residue |
| B | ASP51 |
| B | HIS83 |
| B | HIS109 |
| B | FE401 |
| B | DGI500 |
| B | HOH625 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | HIS21 |
| B | HIS50 |
| B | ASP51 |
| B | ASP127 |
| B | FE400 |
| B | DGI500 |
| B | HOH625 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 B 402 |
| Chain | Residue |
| A | THR15 |
| A | GLU16 |
| A | HIS17 |
| B | GLY0 |
| B | GLY96 |
| B | ILE97 |
| B | GLU98 |
| B | ASP99 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE UNL A 501 |
| Chain | Residue |
| A | TYR77 |
| A | THR110 |
| A | LEU164 |
| A | PRO170 |
| A | ILE171 |
| A | TYR172 |
| A | THR175 |
| A | PO4500 |
| A | HOH661 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 502 |
| Chain | Residue |
| A | PRO12 |
| A | HIS13 |
| A | LEU14 |
| A | THR15 |
| A | PG4506 |
| B | MSE1 |
| B | LYS5 |
| B | VAL95 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 503 |
| Chain | Residue |
| A | ASP31 |
| A | LEU32 |
| A | LEU35 |
| A | ILE129 |
| A | LYS146 |
| A | HOH669 |
| B | LEU35 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 504 |
| Chain | Residue |
| A | LYS166 |
| A | LYS167 |
| A | ASN168 |
| A | GLN169 |
| A | PG4505 |
| A | HOH673 |
| B | GLU67 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 505 |
| Chain | Residue |
| A | LYS166 |
| A | LYS167 |
| A | PG4504 |
| A | HOH671 |
| B | LYS68 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 506 |
| Chain | Residue |
| A | LYS11 |
| A | LEU14 |
| A | GLU16 |
| A | PG4502 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE DGI B 500 |
| Chain | Residue |
| B | PRO170 |
| B | TYR172 |
| B | THR175 |
| B | FE400 |
| B | FE401 |
| B | HOH556 |
| B | HOH609 |
| B | HOH625 |
| B | HOH628 |
| B | HOH654 |
| B | ARG18 |
| B | HIS21 |
| B | ASP51 |
| B | LYS54 |
| B | TYR77 |
| B | GLU80 |
| B | HIS83 |
| B | HIS109 |
| B | THR110 |
| B | ASP127 |
| B | ARG133 |
| B | LEU164 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 501 |
| Chain | Residue |
| B | HIS13 |
| B | TYR52 |
| B | GLU94 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 B 502 |
| Chain | Residue |
| B | LEU35 |
| B | ARG142 |
| B | LYS146 |
| B | HOH622 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2O08","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":"NOV-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of hypothetical protein (NP_242193.1) from Bacillus halodurans at 1.90 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
