2E15
Crystal structure of Arg173 to Asn mutant of Diphthine synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004164 | molecular_function | diphthine synthase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017183 | biological_process | protein histidyl modification to diphthamide |
| A | 0032259 | biological_process | methylation |
| B | 0004164 | molecular_function | diphthine synthase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017183 | biological_process | protein histidyl modification to diphthamide |
| B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1301 |
| Chain | Residue |
| B | ARG46 |
| B | HIS126 |
| B | TYR128 |
| B | HIS243 |
| B | HOH1591 |
| B | HOH1657 |
| B | HOH1681 |
| B | HOH1789 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1302 |
| Chain | Residue |
| B | LYS129 |
| B | LYS241 |
| B | HIS243 |
| B | HOH1533 |
| B | HOH1550 |
| B | HOH1573 |
| B | HOH1661 |
| B | HOH1745 |
| B | ARG46 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1303 |
| Chain | Residue |
| A | ARG60 |
| A | HOH1653 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1304 |
| Chain | Residue |
| A | SER211 |
| A | LEU212 |
| A | ASN213 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1305 |
| Chain | Residue |
| B | PRO257 |
| B | ARG258 |
| B | HOH1773 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1306 |
| Chain | Residue |
| A | PRO257 |
| A | ARG258 |
| A | HOH1563 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 1300 |
| Chain | Residue |
| A | LEU10 |
| A | THR36 |
| A | SER37 |
| A | GLY86 |
| A | ASP87 |
| A | VAL90 |
| A | SER115 |
| A | ILE116 |
| A | PHE165 |
| A | LEU166 |
| A | LEU206 |
| A | ARG208 |
| A | ALA209 |
| A | PRO233 |
| A | HIS234 |
| A | HOH1515 |
| A | HOH1567 |
| A | HOH1569 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES A 1501 |
| Chain | Residue |
| A | PHE34 |
| A | MET39 |
| A | THR42 |
| A | THR43 |
| A | LEU44 |
| A | VAL57 |
| A | HOH1715 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MES B 1502 |
| Chain | Residue |
| B | ASP200 |
| B | TYR220 |
| B | LYS222 |
| B | GLU259 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1401 |
| Chain | Residue |
| B | LEU38 |
| B | MET39 |
| B | THR42 |
| B | THR43 |
| B | LEU44 |
| B | HOH1639 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1402 |
| Chain | Residue |
| A | TYR128 |
| A | HIS243 |
| B | ASN66 |
| B | LYS132 |
| B | GOL1404 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1403 |
| Chain | Residue |
| A | THR43 |
| A | ARG46 |
| A | HOH1699 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1404 |
| Chain | Residue |
| A | GOL1402 |
| B | GLU61 |
| B | LEU65 |
| B | THR135 |
| B | HOH1566 |
| B | HOH1668 |
| B | HOH1685 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18391406","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of diphthine synthase from Pyrococcus horikoshii OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
