Structure of PDB 3nl5 Chain B

Receptor sequence
>3nl5B (length=510) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
KFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNLVQIREKDADTKFF
IEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIRKL
VGPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLFPMGTAGAIRVLDA
LERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICVVSDIIAS
LDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIISNTLKARP
LVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHATLLLNTG
SVAPPEMLKAAIRAYNDVKPIVFDPVGYSATETRLLLNNKLLTFGQFSCI
KGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFIADGTIEGK
YSLSKGTNGTSVEDIPCVAVEAGPIEIMGDITASGCSLGSTIACMIGGQP
SEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTP
VTWAPKLTHT
3D structure
PDB3nl5 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
ChainB
Resolution3.3 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) R41 S110
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 MG B D340 V342 C466 D324 V326 C436
BS02 ACP B N369 T416 G417 E418 D420 I455 M458 A463 S464 G465 K497 N353 T386 G387 E388 D390 I425 M428 A433 S434 G435 K467
BS03 TZE B N272 V274 C466 N257 V259 C436
BS04 TZE B P290 I291 M292 P275 I276 M277
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:3nl5, PDBe:3nl5, PDBj:3nl5
PDBsum3nl5
PubMed20968298
UniProtQ6FV03

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