Structure of PDB 3h9j Chain A

Receptor sequence
>3h9jA (length=339) Species: 562 (Escherichia coli) [Search protein sequence]
MDYILGRYVKIARYGSGGLVGGGGKEQYVENLVLWENIIKTAYCFITPSS
YTAALETANIPEKDFSNCFRFLKENFFIIPGEYNNSTENNRYSRNFLHYQ
SYGANPVLVQDKLKNAKVVILGCGGIGNHVSVILATSGIGEIILIDNDQI
ENTNLTRQVLFSEDDVGKNKTEVIKRELLKRNSEISVSEIALNINDYTDL
HKVPEADIWVVSADHPFNLINWVNKYCVRANQPYINAGYVNDIAVFGPLY
VPGKTGCYECQKKENIDHKIKLINSRFKPATFAPVNNVAAALCAADVIKF
IGKYSEPLSLNKRIGIWSDEIKIHSQNMGRSPVCSVCGN
3D structure
PDB3h9j How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R157
Catalytic site (residue number reindexed from 1) R157
Enzyme Commision number ?
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 peptide A R322 G324 R313 G315
BS02 ZN A C257 C343 C346 C257 C334 C337
BS03 APC A G124 G125 D146 D148 R157 K170 N193 I194 A213 D214 H215 G124 G125 D146 D148 R157 K170 N193 I194 A213 D214 H215
Gene Ontology
Molecular Function
GO:0004792 thiosulfate sulfurtransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008641 ubiquitin-like modifier activating enzyme activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3h9j, PDBe:3h9j, PDBj:3h9j
PDBsum3h9j
PubMed19494832
UniProtQ47506

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