Structure of PDB 5jfm Chain H

Receptor sequence
>5jfmH (length=441) Species: 316056 (Rhodopseudomonas palustris BisB18) [Search protein sequence]
AAVSDGVFETMDAAVEAAALAQQQYLLCSMSDRARFVQGIRDVILNQDTL
EKMSRMAVEETGMGNYEHKLIKNRLAGEKTPGIEDLTTDAFSGDNGLTLV
EYSPFGVIGAITPTTNPTETIVCNSIGMLAAGNSVVFSPHPRARQVSLLL
VRLINQKLAALGAPENLVVTVEKPSIENTNAMMAHPKVRMLVATGGPAIV
KAVLSTGKKAIGAGAGNPPVVVDETANIEKAACDIVNGCSFDNNLPCVAE
KEIIAVAQIADYLIFNLKKNGAYEIKDPAVLQQLQDLVLTAKGGPQTKCV
GKSAVWLLSQIGISVDASIKIILMEVPREHPFVQEELMMPILPLVRVETV
DDAIDLAIEVEHDNRHTAIMHSTDVRKLTKMAKLIQTTIFVKNGPSYAGL
GAGGEGYSTFTIAGPTGEGLTSAKSFARRRKCVMVEALNIR
3D structure
PDB5jfm In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment.
ChainH
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) T115 A213 C247
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 H I194 T198 N199 P222 H223 R225 I259 T262 G278 P329 C330 F493 I111 T115 N116 P139 H140 R142 I176 T179 G195 P246 C247 F410
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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