Structure of PDB 1tka Chain B

Receptor sequence
>1tkaB (length=678) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
QFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNP
TNPDWINRDRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPG
HPEFELPGVEVTTGPLGQGISNAVGMAMAQANLAATYNKPGFTLSDNYTY
VFLGDGCLQEGISSEASSLAGHLKLGNLIAIYDDNKITIDGATSISFDED
VAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDKPTLIKMTTTIGY
GSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKTIL
KPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQLPANWESKLPTYTAK
DSAVATRKLSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSS
GSGNYSGRYIRYGIREHAMGAIMNGISAFGANYKPYGGTFLNFVSYAAGA
VRLSALSGHPVIWVATHDSIGVGEDGPTHQPIETLAHFRSLPNIQVWRPA
DGNEVSAAYKNSLESKHTPSIIALSRQNLPQLEGSSIESASKGGYVLQDV
ANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLEYR
LSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFT
PEGVAERAQKTIAFYKGDKLISPLKKAF
3D structure
PDB1tka Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H30 I250 H263 E418 H481
Catalytic site (residue number reindexed from 1) H28 I248 H261 E416 H479
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 N3T B D382 I416 F445 Y448 H481 D380 I414 F443 Y446 H479 PDBbind-CN: -logKd/Ki=6.10,Kd=0.8uM
BS02 CA B D157 N187 I189 D155 N185 I187
BS03 N3T B H69 L118 N187 I189 T190 I191 H263 H67 L116 N185 I187 T188 I189 H261 PDBbind-CN: -logKd/Ki=6.10,Kd=0.8uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004802 transketolase activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006098 pentose-phosphate shunt
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1tka, PDBe:1tka, PDBj:1tka
PDBsum1tka
PubMed8144674
UniProtP23254|TKT1_YEAST Transketolase 1 (Gene Name=TKL1)

[Back to BioLiP]