Structure of PDB 3h9g Chain D

Receptor sequence
>3h9gD (length=340) Species: 562 (Escherichia coli) [Search protein sequence]
MDYILGRYVKIARYGSGGLVGGGGKEQYVENLVLWENIIKTAYCFITPSS
YTAALETANIPEKDFSNCFRFLKENFFIIPGEYNNNRYSRNFLHYQSYGA
NPVLVQDKLKNAKVVILGCGGIGNHVSVILATSGIGEIILIDNDQIENTN
LTRQVLFSEDDVGKNKTEVIKRELLKRNSEISVSEIALNINDYTDLHKVP
EADIWVVSADHPFNLINWVNKYCVRANQPYINAGYVNDIAVFGPLYVPGK
TGCYECQKVVADLYKENIDHKIKLINSRFKPATFAPVNNVAAALCAADVI
KFIGKYSEPLSLNKRIGIWSDEIKIHSQNMGRSPVCSVCG
3D structure
PDB3h9g How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.
ChainD
Resolution2.2 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) R153
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 D Y14 L19 E26 Y14 L19 E26
BS02 peptide D D214 I220 G238 Y239 Y258 V264 A265 L267 F286 R322 G324 H333 Q335 D210 I216 G234 Y235 Y254 V260 A261 L263 F279 R315 G317 H326 Q328
BS03 ZN D C257 C343 C346 C253 C336 C339
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:3h9g, PDBe:3h9g, PDBj:3h9g
PDBsum3h9g
PubMed19494832
UniProtQ47506

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