PDBsum entry 2e8r

Transferase

PDB id: 2e8r

Contents

Protein chains

265 a.a. *

Ligands

SAH

Metals

_NA

Waters ×536

* Residue conservation analysis

PDB id:

2e8r

Name:

Transferase

Title:

Structural study of project id ph0725 from pyrococcus horikoshii ot3

Structure:

Probable diphthine synthase. Chain: a, b. Synonym: diphthamide biosynthesis methyltransferase. Engineered: yes. Mutation: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.193 R-free: 0.218

Authors:

Y.Asada,M.Taketa,H.Shimada,Y.Matsuura,N.Kunishima,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

Y.Asada et al. Structural study of project id ph0725 from pyrococcus horikoshii ot3. To be published, .

Date:

23-Jan-07 Release date: 24-Jul-07

Protein chains

O58456  (DPHB_PYRHO) -  Diphthine synthase from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: 265 a.a.

Struc: 265 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.1.1.98 - diphthine synthase.
• Reaction: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 S-adenosyl-L-homocysteine + 3 H⁺

2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 × S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 × S-adenosyl-L-homocysteine + 3 × H(+) (Bound ligand (Het Group name = SAH) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site