Structure of PDB 5jfm Chain E

Receptor sequence
>5jfmE (length=439) Species: 316056 (Rhodopseudomonas palustris BisB18) [Search protein sequence]
VSDGVFETMDAAVEAAALAQQQYLLCSMSDRARFVQGIRDVILNQDTLEK
MSRMAVEETGMGNYEHKLIKNRLAGEKTPGIEDLTTDAFSGDNGLTLVEY
SPFGVIGAITPTTNPTETIVCNSIGMLAAGNSVVFSPHPRARQVSLLLVR
LINQKLAALGAPENLVVTVEKPSIENTNAMMAHPKVRMLVATGGPAIVKA
VLSTGKKAIGAGAGNPPVVVDETANIEKAACDIVNGCSFDNNLPCVAEKE
IIAVAQIADYLIFNLKKNGAYEIKDPAVLQQLQDLVLTAKGGPQTKCVGK
SAVWLLSQIGISVDASIKIILMEVPREHPFVQEELMMPILPLVRVETVDD
AIDLAIEVEHDNRHTAIMHSTDVRKLTKMAKLIQTTIFVKNGPSYAGLGA
GGEGYSTFTIAGPTGEGLTSAKSFARRRKCVMVEALNIR
3D structure
PDB5jfm In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment.
ChainE
Resolution2.516 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T198 A296 C330
Catalytic site (residue number reindexed from 1) T113 A211 C245
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 1VU E N199 S221 P222 H223 R225 I259 T277 G278 P329 C330 T380 F493 N114 S136 P137 H138 R140 I174 T192 G193 P244 C245 T295 F408
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008774 acetaldehyde dehydrogenase (acetylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:5jfm, PDBe:5jfm, PDBj:5jfm
PDBsum5jfm
PubMed28202954
UniProtQ21A49

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