Structure of PDB 4b0t Chain B

Receptor sequence
>4b0tB (length=472) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
STVESALTRRIMGIETEYGLTFVDLRPDEIARRMFRPIVEKYSSSNIFIP
NGSRLYLDVGSHPEYATAECDNLTQLINFEKAGDVIADRMAVDAEESLAK
EDIAGQVYLFKNNVDSVGNSYGCHENYLVGRSMPLKALGKRLMPFLITRQ
LICGAGRIHHPNPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINT
RDEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEMIEADFGLPS
LELANDIASIREISRDATGSTLLSLKDGTTMTALQIQQVVFEHASKWLEQ
RPEPEFSGTSNTEMARVLDLWGRMLKAIESGDFSEVDTEIDWVIKKKLID
RFIQRGNLGLDDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAI
LAAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNRPEPQSVELG
DPFSAVNSEVDQLIEYMTVHAE
3D structure
PDB4b0t Structures of Pup Ligase Pafa and Depupylase Dop from the Prokaryotic Ubiquitin-Like Modification Pathway.
ChainB
Resolution2.159 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.19: prokaryotic ubiquitin-like protein ligase.
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 ADP B I12 E16 P450 I11 E15 P444
BS02 ADP B R60 T73 E75 N132 L134 P210 H211 R219 W440 P458 R54 T67 E69 N126 L128 P204 H205 R213 W434 P452
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0019787 ubiquitin-like protein transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0010498 proteasomal protein catabolic process
GO:0019941 modification-dependent protein catabolic process
GO:0070490 protein pupylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4b0t, PDBe:4b0t, PDBj:4b0t
PDBsum4b0t
PubMed22910360
UniProtQ8NQE1|PAFA_CORGL Pup--protein ligase (Gene Name=pafA)

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