4BNQ
The structure of the Staphylococcus aureus Ham1 protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009143 | biological_process | nucleoside triphosphate catabolic process |
| A | 0009146 | biological_process | purine nucleoside triphosphate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
| A | 0035870 | molecular_function | dITP diphosphatase activity |
| A | 0036220 | molecular_function | ITP diphosphatase activity |
| A | 0036222 | molecular_function | XTP diphosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0009143 | biological_process | nucleoside triphosphate catabolic process |
| B | 0009146 | biological_process | purine nucleoside triphosphate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017111 | molecular_function | ribonucleoside triphosphate phosphatase activity |
| B | 0035870 | molecular_function | dITP diphosphatase activity |
| B | 0036220 | molecular_function | ITP diphosphatase activity |
| B | 0036222 | molecular_function | XTP diphosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 800 |
| Chain | Residue |
| A | SER8 |
| A | HOH2009 |
| A | HOH2010 |
| A | ASN9 |
| A | ASN10 |
| A | LYS13 |
| A | GLU40 |
| A | LYS52 |
| A | ASP67 |
| A | HOH2003 |
| A | HOH2004 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 801 |
| Chain | Residue |
| A | GLU3 |
| A | LYS62 |
| A | THR108 |
| A | THR109 |
| A | ASP110 |
| A | HOH2131 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 802 |
| Chain | Residue |
| A | SER136 |
| A | LYS159 |
| A | HOH2084 |
| A | HOH2085 |
| A | HOH2107 |
| A | HOH2132 |
| A | HOH2133 |
| B | SER136 |
| B | LYS159 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 804 |
| Chain | Residue |
| A | HOH2001 |
| A | HOH2058 |
| A | HOH2128 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 803 |
| Chain | Residue |
| B | SER8 |
| B | ASN9 |
| B | LYS13 |
| B | HOH2003 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 901 |
| Chain | Residue |
| B | THR44 |
| B | PHE45 |
| B | GLU72 |
| B | LYS132 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01405","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01405","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
