Structure of PDB 5jfn Chain C

Receptor sequence
>5jfnC (length=446) Species: 316056 (Rhodopseudomonas palustris BisB18) [Search protein sequence]
KSPDGKSVSDGVFETMDAAVEAAALAQQQYLLCSMSDRARFVQGIRDVIL
NQDTLEKMSRMAVEETGMGNYEHKLIKNRLAGEKTPGIEDLTTDAFSGDN
GLTLVEYSPFGVIGAITPTTNPTETIVCNSIGMLAAGNSVVFSPHPRARQ
VSLLLVRLINQKLAALGAPENLVVTVEKPSIENTNAMMAHPKVRMLVATG
GPAIVKAVLSTGKKAIGAGAGNPPVVVDETANIEKAACDIVNGCSFDNNL
PCVAEKEIIAVAQIADYLIFNLKKNGAYEIKDPAVLQQLQDLVLTAKGGP
QTKCVGKSAVWLLSQIGISVDASIKIILMEVPREHPFVQEELMMPILPLV
RVETVDDAIDLAIEVEHDNRHTAIMHSTDVRKLTKMAKLIQTTIFVKNGP
SYAGLGAGGEGYSTFTIAGPTGEGLTSAKSFARRRKCVMVEALNIR
3D structure
PDB5jfn In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment.
ChainC
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) T120 A218 C252
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 C I194 P196 T197 T198 N199 H223 R225 I259 T262 T277 G278 X330 T380 I116 P118 T119 T120 N121 H145 R147 I181 T184 T199 G200 X252 T302
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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