2E8H
Crystal structure of PH0725 from Pyrococcus horikoshii OT3
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 | 6 |
Details | BINDING SITE FOR RESIDUE NA A 401 |
Chain | Residue |
A | TYR117 |
A | HOH1304 |
A | HOH1314 |
B | GLY131 |
B | HOH268 |
B | HOH271 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH A 1301 |
Chain | Residue |
A | ASP87 |
A | VAL90 |
A | SER115 |
A | ILE116 |
A | PHE165 |
A | LEU166 |
A | ARG208 |
A | ALA209 |
A | PRO233 |
A | HIS234 |
A | ILE235 |
A | HOH1315 |
A | HOH1349 |
A | HOH1400 |
A | LEU10 |
A | THR36 |
A | SER37 |
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 |