Structure of PDB 8irk Chain A

Receptor sequence
>8irkA (length=379) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
LVPRGSHMMMLAQQWRDARPKVAGLHLDSGACSRQSFAVIDATTAHARHE
AEVGGYVAAEAATPALDAGRAAVASLIGFAASDVVYTSGSNHAIDLLLSS
WPGKRTLACLPGEYGPNLSAMAANGFQVRALPVDDDGRVLVDEASHELSA
HPVALVHLTALASHRGIAQPAAELVEACHNAGIPVVIDAAQALGHLDCNV
GADAVYSSSRKWLAGPRGVGVLAVRPELAERLQPRIPPSDWPIPMSVLEK
LELGEHNAAARVGFSVAVGEHLAAGPTAVRERLAEVGRLSRQVLAEVDGW
RVVEPVDQPTAITTLESTDGADPASVRSWLIAERGIVTTACELARAPFEM
RTPVLRISPHVDVTVDELEQFAAALREAP
3D structure
PDB8irk Structure of Mycobacterial ergothioneine-biosynthesis C-S lyase EgtE
ChainA
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.-.-
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 PLP A G81 S82 N83 Y106 D180 A182 Q183 S200 R202 K203 G89 S90 N91 Y114 D188 A190 Q191 S208 R210 K211
BS02 PYR A G22 A23 K203 R337 R348 G30 A31 K211 R345 R356
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:1990411 hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
Biological Process
GO:0052699 ergothioneine biosynthetic process
GO:0052704 ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide

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Molecular Function
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Biological Process
External links
PDB RCSB:8irk, PDBe:8irk, PDBj:8irk
PDBsum8irk
PubMed38072054
UniProtA0R5M7|EGTE_MYCS2 Probable hercynylcysteine sulfoxide lyase (Gene Name=egtE)

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