2DVN
Structure of PH1917 protein with the complex of IMP from Pyrococcus horikoshii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1202 |
| Chain | Residue |
| A | SER82 |
| A | ARG86 |
| A | IMP1301 |
| A | HOH1471 |
| A | HOH1498 |
| A | HOH1564 |
| A | HOH1573 |
| A | HOH1578 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1203 |
| Chain | Residue |
| A | SER8 |
| A | ASN9 |
| A | LYS12 |
| A | TYR34 |
| A | GLU36 |
| A | GLU64 |
| A | IMP1301 |
| A | HOH1436 |
| A | HOH1458 |
| A | HOH1471 |
| A | HOH1486 |
| A | HOH1573 |
| A | HOH1643 |
| A | THR7 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1204 |
| Chain | Residue |
| A | LYS41 |
| A | TYR106 |
| A | LYS108 |
| A | LYS118 |
| A | HOH1447 |
| A | HOH1570 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1207 |
| Chain | Residue |
| A | TYR85 |
| A | PHE140 |
| A | GLY141 |
| A | HOH1506 |
| A | HOH1545 |
| A | HOH1639 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1208 |
| Chain | Residue |
| A | ARG14 |
| A | HIS138 |
| A | THR159 |
| A | ILE160 |
| A | GOL1431 |
| A | HOH1444 |
| A | HOH1589 |
| B | TRP179 |
| B | ASN183 |
| B | HOH1445 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1211 |
| Chain | Residue |
| A | GLY89 |
| A | LEU90 |
| A | GLU91 |
| A | LYS134 |
| A | HOH1534 |
| A | HOH1624 |
| A | HOH1664 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1212 |
| Chain | Residue |
| A | ARG129 |
| A | SER131 |
| A | ASN132 |
| A | ARG135 |
| A | HOH1500 |
| A | HOH1552 |
| A | HOH1641 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1213 |
| Chain | Residue |
| A | ASN164 |
| A | LYS174 |
| A | HOH1445 |
| A | HOH1528 |
| A | HOH1652 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1214 |
| Chain | Residue |
| A | HIS32 |
| A | TRP52 |
| A | LYS56 |
| A | HOH1659 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1205 |
| Chain | Residue |
| B | GLY89 |
| B | LEU90 |
| B | GLU91 |
| B | LYS134 |
| B | HOH1506 |
| B | HOH1507 |
| B | HOH1519 |
| B | HOH1594 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1206 |
| Chain | Residue |
| B | SER72 |
| B | GLY99 |
| B | ALA100 |
| B | GLU101 |
| B | ASP102 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1209 |
| Chain | Residue |
| B | TYR85 |
| B | PHE140 |
| B | GLY141 |
| B | HOH1501 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1210 |
| Chain | Residue |
| B | SER151 |
| B | GLU152 |
| B | LYS153 |
| B | HOH1615 |
| site_id | BC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IMP A 1301 |
| Chain | Residue |
| A | ASP143 |
| A | LYS163 |
| A | HIS168 |
| A | ARG169 |
| A | SO41202 |
| A | SO41203 |
| A | HOH1438 |
| A | HOH1458 |
| A | HOH1493 |
| A | HOH1498 |
| A | HOH1564 |
| A | LYS12 |
| A | GLU36 |
| A | GLU64 |
| A | ASP65 |
| A | SER66 |
| A | SER81 |
| A | SER82 |
| A | PHE107 |
| A | PHE140 |
| A | GLY141 |
| A | TYR142 |
| site_id | BC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IMP B 1302 |
| Chain | Residue |
| B | LYS12 |
| B | GLU64 |
| B | ASP65 |
| B | SER66 |
| B | SER81 |
| B | SER82 |
| B | PHE107 |
| B | PHE140 |
| B | TYR142 |
| B | ASP143 |
| B | LYS163 |
| B | HIS168 |
| B | ARG169 |
| B | HOH1511 |
| B | HOH1586 |
| B | HOH1593 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1431 |
| Chain | Residue |
| A | HIS138 |
| A | GLY139 |
| A | SO41208 |
| A | HOH1451 |
| A | HOH1469 |
| A | HOH1557 |
| B | GLU178 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1432 |
| Chain | Residue |
| B | THR7 |
| B | SER8 |
| B | ASN9 |
| B | LYS12 |
| B | GLU36 |
| B | HOH1440 |
| B | HOH1516 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1433 |
| Chain | Residue |
| A | VAL125 |
| A | LYS171 |
| A | LYS181 |
| A | HOH1565 |
| A | HOH1672 |
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 | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18062990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Structure of nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"2DVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E5X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18062990","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZTI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
