Structure of PDB 6q2e Chain B

Receptor sequence
>6q2eB (length=329) Species: 2173 (Methanobrevibacter smithii) [Search protein sequence]
SMYNMDLDKVIRKINKKGARTVGLQFPEGLKMQAVKIAKAIESQTPATVI
ISGDPCFGACDVSDYKMKGSVDLIVHYGHTPLPLKYEVPTLFIEAFSNID
VKKDLEKCLEKLEDYSKIALVTTTQHLHLLNEIKDYLEDNGKEVVLGSSK
NTKKGQVLGCNFSSIKNLDAEVYLFIGSGNFHPLGIYLFTKSPVLALDPY
NSEIRDISAFADRILRIRFARITKAREAEKWGIIVSSKEGQYRMKLAKEI
KKILEDNKMEAYIIMADNINPDILLPYMELDAFVVSACPRIAIDDSQMYK
KPLLTPQELEIVLNKRQWENYQLDEILFH
3D structure
PDB6q2e The Crystal Structure of Dph2 in Complex with Elongation Factor 2 Reveals the Structural Basis for the First Step of Diphthamide Biosynthesis.
ChainB
Resolution1.768 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.108: 2-(3-amino-3-carboxypropyl)histidine synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MTA B F58 K239 Q242 N269 I270 C289 R291 I292 D295 D296 F57 K238 Q241 N268 I269 C288 R290 I291 D294 D295
BS02 SF4 B F58 C61 G160 C161 C289 R291 F57 C60 G159 C160 C288 R290
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0090560 2-(3-amino-3-carboxypropyl)histidine synthase activity
Biological Process
GO:0017183 protein histidyl modification to diphthamide

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Molecular Function
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Biological Process
External links
PDB RCSB:6q2e, PDBe:6q2e, PDBj:6q2e
PDBsum6q2e
PubMed31566354
UniProtA5UMY5

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