Structure of PDB 4h0v Chain A

Receptor sequence
>4h0vA (length=413) Species: 1502 (Clostridium perfringens) [Search protein sequence]
AFIERPEDFLKDKENAIQWEKKEAERVEKNLDTLEKEALELYKKDSEQIS
NYSQTRQYFYDYQIESNPREKEYKNLRNAISKNKIDKPINVYYFESPEKF
AFNKEIRTENQNEISLEKFNELKETIQDKLFKQDGFKDVSLYEPGNGDEK
PTPLLIHLKLPKNTGMLPYINSNDVKTLIEQDYSIKIDKIVRIVIEGKQY
IKAEASIVNSLDFKDDVSKGDLWGKENYSDWSNKLTPNELADVNDYMRGG
YTAINNYLISNGPLNNPNPELDSKVNNIENALKLTPIPSNLIVYRRSGPQ
EFGLTLTSPEYDFNKIENIDAFKEKWEGKVITYPNFISTSIGSVNMSAFA
KRKIILRINIPKDSPGAYLSAIPGYAGSYEVLLNHGSKFKINKVDSYKDG
TVTKLILDATLIN
3D structure
PDB4h0v Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex
ChainA
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K176
Catalytic site (residue number reindexed from 1) K176
Enzyme Commision number 2.4.2.31: NAD(+)--protein-arginine ADP-ribosyltransferase.
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 NAD A Y251 R295 R296 G298 Q300 E301 N335 T339 F349 R352 E380 Y251 R295 R296 G298 Q300 E301 N335 T339 F349 R352 E380
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:4h0v, PDBe:4h0v, PDBj:4h0v
PDBsum4h0v
PubMed23382240
UniProtQ46220

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