Structure of PDB 3nl6 Chain A

Receptor sequence
>3nl6A (length=518) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
KFSKEQFDYSLYLVTSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADTK
FFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIR
KLVGPDMVIGWSVGFPEEVDELSKMGPVDYIGVGTLFPTLTKKAPMGTAG
AIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICV
VSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIIS
NTLKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHA
TLLLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNKLL
TFGQFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFI
ADGTIEGKYSLSKGTNGTSVEDIPCVAVEAGPIEIMGDITASGCSLGSTI
ACMIGGQPSEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALY
RLTRENTPVTWAPKLTHT
3D structure
PDB3nl6 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
ChainA
Resolution2.612 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R45 S114
Catalytic site (residue number reindexed from 1) R43 S112
Enzyme Commision number 2.5.1.3: thiamine phosphate synthase.
2.7.1.50: hydroxyethylthiazole kinase.
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 TPS A Q43 R45 H90 S114 T139 T143 T145 I179 V209 S210 Q41 R43 H88 S112 T135 T139 T141 I171 V201 S202
BS02 ACP A N369 T416 G417 E418 D420 I455 M458 A463 S464 G465 Y496 K497 N361 T394 G395 E396 D398 I433 M436 A441 S442 G443 Y474 K475
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004417 hydroxyethylthiazole kinase activity
GO:0004789 thiamine-phosphate diphosphorylase activity
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009228 thiamine biosynthetic process
GO:0009229 thiamine diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
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:3nl6, PDBe:3nl6, PDBj:3nl6
PDBsum3nl6
PubMed20968298
UniProtQ6FV03

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