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 | 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 | 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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01405 |
Chain | Residue | Details |
A | ASP68 | |
B | ASP68 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01405 |
Chain | Residue | Details |
A | SER8 | |
B | ASP68 | |
B | SER69 | |
B | PHE149 | |
B | LYS172 | |
B | HIS177 | |
A | GLU39 | |
A | ASP68 | |
A | SER69 | |
A | PHE149 | |
A | LYS172 | |
A | HIS177 | |
B | SER8 | |
B | GLU39 |