Structure of PDB 4zfl Chain J

Receptor sequence
>4zflJ (length=229) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
ARHVAWLGAPRSLADLVLDPPQGLLVQSYAPRRQKHGLMNADGWGAGFFD
DDGVARRWRSDKPLWGDASFASVAPALRSRCVVAAVRSATIGMPIEPSAS
APFSDGQWLLSHNGLVDRGVLPLTGAAESTVDSAILAALIFSRGLDALGA
TIAEVGELDPNARLNILAANGSRLLATTWGDTLSVLRRPDGVVLASEPYD
DDPGWSDIPDRHLVDVRDAHVVVTPLLEH
3D structure
PDB4zfl Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.
ChainJ
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.118: gamma-glutamyl hercynylcysteine S-oxide hydrolase.
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 4NK J Y30 W66 Y29 W65
BS02 4NK J H37 G38 L39 M40 R88 S89 A90 G115 L116 V132 D133 S134 R164 H36 G37 L38 M39 R87 S88 A89 G114 L115 V131 D132 S133 R163
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Biological Process
GO:0006541 glutamine metabolic 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:4zfl, PDBe:4zfl, PDBj:4zfl
PDBsum4zfl
PubMed26079795
UniProtA0R5M9|EGTC_MYCS2 Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase (Gene Name=egtC)

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