Structure of PDB 6s7q Chain E

Receptor sequence
>6s7qE (length=497) Species: 158 (Treponema denticola) [Search protein sequence]
DALILTGKPLSLEDVYSVAYNNRQVKISDDAEERVKKARQILFDMAAEGK
PVYGLNRGVGWNKDKEFDEDFFATYNRNLLNSHCLGVKPYHPDEQVRAIL
LLRLNKALTGHTGISAELLHHYRDFLNYGIHPRIPMRSSIGEGDITTLSH
IGLAFIGEEDVSFNGEIMNSKKAMEKAGLKPAKLGPKDGLSIVSCNAQGE
AMTAIVLKEIEDLVYMSNLIFCLSLEGLNGVVQSLREDVNAVRGIKGQIK
AAEMCREFLKGSFLYDPDPERALQDPLSFRCAHSVNGTMYDAMDYVREQL
LTTMNTTDDNPCIIIDEHSSFVSANFEITSLAIGVEMLATALSHLSKTSC
YRMIKLADPSFTKLNRFLTPQDVKTIAFGTIQKTFTMLDTQNRGLANPSS
MDFYSLAGTIEDHASNLPLACYKIFQMLDNIRYIIGIEAMHAAQAIDLRG
NKKLGEGTKKAYSLIREVLPFYNEDRNISRDIETMYEFIKSKKLLNI
3D structure
PDB6s7q Structure and Mechanism of Ergothionase from Treponema denticola.
ChainE
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y54 G61 D276 A325
Catalytic site (residue number reindexed from 1) Y53 G60 D275 A324
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 KZ5 E G380 T381 K384 G379 T380 K383
BS02 KZ5 E H84 E143 I146 E412 H83 E142 I145 E411
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004397 histidine ammonia-lyase activity
GO:0016841 ammonia-lyase activity
Biological Process
GO:0006548 L-histidine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6s7q, PDBe:6s7q, PDBj:6s7q
PDBsum6s7q
PubMed31188501
UniProtM2BPW8

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