2E5X
Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | TYR34 |
| A | GLU36 |
| A | GLU64 |
| A | ASP65 |
| A | ITT201 |
| A | NA302 |
| A | HOH595 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 302 |
| Chain | Residue |
| A | NA301 |
| A | NA303 |
| A | HOH450 |
| A | HOH580 |
| A | GLU36 |
| A | ITT201 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 303 |
| Chain | Residue |
| A | GLU36 |
| A | ASP65 |
| A | ITT201 |
| A | NA302 |
| A | HOH413 |
| A | HOH445 |
| A | HOH579 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ITT A 201 |
| Chain | Residue |
| A | THR7 |
| A | SER8 |
| A | ASN9 |
| A | LYS12 |
| A | GLU36 |
| A | GLU64 |
| A | ASP65 |
| A | SER66 |
| A | SER81 |
| A | SER82 |
| A | TYR85 |
| A | PHE107 |
| A | PHE140 |
| A | GLY141 |
| A | TYR142 |
| A | ASP143 |
| A | LYS163 |
| A | HIS168 |
| A | ARG169 |
| A | NA301 |
| A | NA302 |
| A | NA303 |
| A | HOH414 |
| A | HOH440 |
| A | HOH450 |
| A | HOH551 |
| A | HOH580 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | GLU43 |
| A | LYS121 |
| A | SER123 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | PRO58 |
| A | PHE69 |
| A | ILE70 |
| A | GLU71 |
| A | GLY75 |
| A | TYR106 |
| A | HOH550 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01405 |
| Chain | Residue | Details |
| A | ASP65 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18062990, ECO:0000269|Ref.2, ECO:0007744|PDB:2DVO, ECO:0007744|PDB:2E5X |
| Chain | Residue | Details |
| A | PHE140 | |
| A | LYS163 | |
| A | HIS168 | |
| A | THR7 | |
| A | SER66 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18062990, ECO:0007744|PDB:2ZTI |
| Chain | Residue | Details |
| A | ASP65 | |
| A | GLU36 |
