Structure of PDB 6eac Chain C

Receptor sequence
>6eacC (length=475) Species: 317 (Pseudomonas syringae) [Search protein sequence]
MKALDELVFDNRFARLGDAFSTHVLPEPIDAPRLVVASESALALLDLAPE
QSELPLFAEIFSGHKLWAEAEPRAMVYSGHQFGSYNPRLGDGRGLLLGEV
YNDAGEHWDLHLKGAGRTPYSRMGDGRAVLRSSIREFLASEALHALGIPS
SRAACVVSSNTPVWREKQEYAAMVLRLAQSHVRFGSLEYLFYTKQPEHLK
TLAEHVLTMHYPHCQEQPEPYLAMFREIVERNAELIAKWQAYGFCHGVMN
TDNMSILGITFDFGPFAFLDDFDEHFICNHSDHEGRYSFSNQVPIAQWNL
SALGQALTPFVSVEALRETIGLFLPLYQAHYLDLMRRRLGLTVAQDQDDK
LVSQLLQLMQNSGVDYTLFFRRLGDQPAAQALRALRDDFVDIKVFDDWAQ
AYQARIAAEENGTEQARKERMHAVNPLYILRNYLAQNAIEAAEKGDYEEV
RRLHQVLCTPFTEQPGMEGYAQRPP
3D structure
PDB6eac Protein AMPylation by an Evolutionarily Conserved Pseudokinase.
ChainC
Resolution2.269 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.108: protein adenylyltransferase.
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 MG C N253 D262 N253 D262
BS02 CA C S362 G363 D388 S362 G363 D388
BS03 ANP C Y77 G90 G92 R93 K113 R122 G124 D125 G126 R176 R183 N253 D262 Y77 G90 G92 R93 K113 R122 G124 D125 G126 R176 R183 N253 D262
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0070733 AMPylase activity
Biological Process
GO:0018117 protein adenylylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6eac, PDBe:6eac, PDBj:6eac
PDBsum6eac
PubMed30270044
UniProtQ87VB1|SELO_PSESM Protein adenylyltransferase SelO (Gene Name=selO)

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