Structure of PDB 5jfn Chain B

Receptor sequence
>5jfnB (length=439) Species: 316056 (Rhodopseudomonas palustris BisB18) [Search protein sequence]
VSDGVFETMDAAVEAAALAQQQYLLCSMSDRARFVQGIRDVILNQDTLEK
MSRMAVEETGMGNYEHKLIKNRLAGEKTPGIEDLTTDAFSGDNGLTLVEY
SPFGVIGAITPTTNPTETIVCNSIGMLAAGNSVVFSPHPRARQVSLLLVR
LINQKLAALGAPENLVVTVEKPSIENTNAMMAHPKVRMLVATGGPAIVKA
VLSTGKKAIGAGAGNPPVVVDETANIEKAACDIVNGCSFDNNLPCVAEKE
IIAVAQIADYLIFNLKKNGAYEIKDPAVLQQLQDLVLTAKGGPQTKCVGK
SAVWLLSQIGISVDASIKIILMEVPREHPFVQEELMMPILPLVRVETVDD
AIDLAIEVEHDNRHTAIMHSTDVRKLTKMAKLIQTTIFVKNGPSYAGLGA
GGEGYSTFTIAGPTGEGLTSAKSFARRRKCVMVEALNIR
3D structure
PDB5jfn In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment.
ChainB
Resolution1.9 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 COA B I194 P196 T197 N199 P222 H223 T262 T277 G278 X330 T380 I109 P111 T112 N114 P137 H138 T177 T192 G193 X245 T295
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:5jfn, PDBe:5jfn, PDBj:5jfn
PDBsum5jfn
PubMed28202954
UniProtQ21A49

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