Structure of PDB 4bjr Chain B

Receptor sequence
>4bjrB (length=494) Species: 196627 (Corynebacterium glutamicum ATCC 13032) [Search protein sequence]
TVESALTRRIMGIETEYGLTFVDGDSKKLRPDEIARRMFRPIVEKYSSSN
IFIPNGSRLYLNVGSHPEYATAECDNLTQLINFEKAGDVIADRMAVDAEE
SLAKEDIAGQVYLFKNNVDSVGNSYGCHENYLVGRSMPLKALGKRLMPFL
ITRQLICGAGRIHHPNPSFPLGYCISQRSDHVWEGVSSASRPIINTRDEP
HADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEMIEADFGLPSLELA
NDIASIREISRDATGSTLLSLKDGTTMTALQIQQVVFEHASKWLEQRPEP
EFSGTSNTEMARVLDLWGRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQ
RGNLGLDDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAILAAV
DTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNRPEPQSVELGDPFS
AVNSEVDQLIEYMTVHASLLDEIDGLLENNAEEFVRSYVQKGGE
3D structure
PDB4bjr Crystal Structure of the Complex between Prokaryotic Ubiquitin-Like Protein Pup and its Ligase Pafa.
ChainB
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.19: prokaryotic ubiquitin-like protein ligase.
6.3.2.-
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 ATP B I12 G14 I15 E16 R60 Y62 T73 E75 N132 L134 P210 H211 R219 W440 I10 G12 I13 E14 R58 Y60 T71 E73 N130 L132 P200 H201 R209 W430
BS02 MG B E16 Y62 E70 E14 Y60 E68
BS03 MG B E16 H221 E14 H211
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:0031386 protein tag activity
GO:0046872 metal ion binding
GO:0070628 proteasome 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

View graph for
Biological Process
External links
PDB RCSB:4bjr, PDBe:4bjr, PDBj:4bjr
PDBsum4bjr
PubMed23601177
UniProtQ8NQE0;
Q8NQE1|PAFA_CORGL Pup--protein ligase (Gene Name=pafA)

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