Structure of PDB 7wrr Chain A

Receptor sequence
>7wrrA (length=650) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
KETRDLETLSVNAIRFLAIDAVEKARSGHPGMPMGMAPLAYLLFREVMRH
NPLDPDWPDRDRFVLSAGHGSMLLYAVLHLTGYDLPLEELKSFRQWGSKT
PGHPERGHTPGVEVTTGPLGQGISTAVGLALAERKLAAEFNRPGHVVVDH
YTYVLASDGDLMEGVSGEAASLAGHWGLSKLIVFWDDNRISIDGPTDLAF
TEDVLARYRAYGWQTLRVEDVNDLEALRKAIKLAKLDERPTLIAVRSHIG
FGSPKQDSAKAHGEPLGPEAVEATRRNLGWPYPPFVVPEEVYRHMDMREK
GRAWQEAWEKALEAYARAYPDLHQELMRRLRGELPPLPEEPPSFDKPIAT
RAASGRALNLLAPRLPELLGGSADLTPSNNTKAEGMEDFSRANPLGRYLH
FGVREHAMGAILNGLNLHGGYRAYGGTFLVFSDYMRPAIRLAALMGVPTV
FVFTHDSIALGEDGPTHQPVEHLMSLRAMPNLFVIRPADAYETFYAWLVA
LRRKEGPTALVLTRQAVPLLSPEKARGLLRGGYVLEDVEEPQGVLVATGS
EVHLALRAQALLREKGVRVRVVSLPSFELFAAQPEAYRKEVLPPGLPVVA
VEAGASLGWERYAHKVVALDRFGASAPYPEVYERLGFTPERVAEAFLSLV
3D structure
PDB7wrr Structural and biochemical characterizations of Thermus thermophilus HB8 transketolase producing a heptulose.
ChainA
Resolution2.01 Å
3D
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
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 M33 H70 G118 L120 S158 D159 G160 N189 I191 I193 I250 H263 M32 H69 G117 L119 S157 D158 G159 N188 I190 I192 I249 H262
BS02 CA A D159 N189 I191 D158 N188 I190
BS03 TPP A D375 E406 F432 Y435 D374 E405 F431 Y434
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7wrr, PDBe:7wrr, PDBj:7wrr
PDBsum7wrr
PubMed36441206
UniProtQ5SM35

[Back to BioLiP]