Structure of PDB 5jfm Chain D

Receptor sequence
>5jfmD (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.
ChainD
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 D I194 T198 N199 S221 P222 H223 R225 I259 T262 G278 P329 C330 V331 I495 I109 T113 N114 S136 P137 H138 R140 I174 T177 G193 P244 C245 V246 I410
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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