Structure of PDB 6bxk Chain B

Receptor sequence
>6bxkB (length=337) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFL
HGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVS
VVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRG
DSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAID
PYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRI
VKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDWRKPVLT
PKEVEILLGLREEYEFDEILGGPRESDEPFGISIHST
3D structure
PDB6bxk Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis.
ChainB
Resolution2.347 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 Y56 Q241 D268 V269 R289 V290 Y56 Q241 D268 V269 R289 V290
BS02 SF4 B Y56 C59 G162 C163 Q241 C287 Y56 C59 G162 C163 Q241 C287
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
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
GO:0050843 S-adenosylmethionine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6bxk, PDBe:6bxk, PDBj:6bxk
PDBsum6bxk
PubMed29590073
UniProtO58832|DPH2_PYRHO 2-(3-amino-3-carboxypropyl)histidine synthase (Gene Name=dph2)

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