Structure of PDB 8r3p Chain A

Receptor sequence
>8r3pA (length=672) Species: 1352 (Enterococcus faecium) [Search protein sequence]
MFDKIDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVN
PTTSKNWADRDRFVLSAGHGSAMLYSLLHLAGYQVTIDDLKQFRQWDSKT
PGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNKENFNVMDH
YTYAICGDGDLMEGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAF
TENVGARYEAYGWQHILVKDGNDLEAISKAIEEAKAETDKPTLIEVKTVI
GYGAPKEGTSAVHGAPLGEDGIKMAKEVYGWEYPDFTVPEEVAARFHQTM
IEEGQKAEDAWNEMFANYKKAYPELAQQFEDAFDGKLPENWDAELPTYEV
GSSQASRVSSKEVIQELSKAIPSFWGGSADLSGSNNTMVAADKDFTPEHY
EGRNIWFGVREFAMASAMNGIQLHGGTRIYGGTFFVFVDYLRPAVRLAAI
QHTPVVYVLTHDSVAVGEDGPTHEPIEQLASVRCMPGVQVIRPADGNETR
AAWKVAMETTDAPTILVLSRQNLPVLPSTKEVADEMVKKGAYVLSPSQGE
TPEGILIATGSEVDLAVKAQKELAEKGKDVSVVSMPSFDLFEKQSSEYKE
SVLPKSVKKRVAIEAAASFGWERYVGTEGATITIDHFGASAPGTKILEEF
GFTVENVVNTYNQLSENLYFQG
3D structure
PDB8r3p Are Transketolases relevant Targets fighting Human Pathogens? A comparative Biochemical, Bioinformatic and Structural Study
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.2.1.1: transketolase.
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 TPP A H69 L119 D158 G159 N188 I190 L192 H263 H69 L119 D158 G159 N188 I190 L192 H263
BS02 MG A D158 N188 I190 D158 N188 I190
BS03 TPP A E411 F437 Y440 E411 F437 Y440
Gene Ontology
Molecular Function
GO:0004802 transketolase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006098 pentose-phosphate shunt
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8r3p, PDBe:8r3p, PDBj:8r3p
PDBsum8r3p
PubMed
UniProtA0A133CKH8

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