Structure of PDB 3tno Chain A

Receptor sequence
>3tnoA (length=320) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
QKSVLEQLKQVTMVVADTGDFELIKKYKPVDATTNPSLILKAVKEQKYSN
LVAETISKVKANNPDLNSDDLVKEIAIEILVSFGIKILDVIEGKVSSEVD
ARVSFNSATTIDYAKRIIARYESNGIPKDRVLIKIAATWEGIKAAKLLQK
EGINCNLTLIFDKAQAKACAEAGVYLVSPFVGRITDWQMQQNNLKTFPAI
ADDDGVNSVKAIYKLYKSHGFKTIVMGASFRNVEQVIALAGCDALTISPV
LLEELKNRDEHLEVKLTKNDDVVTQSPQISEADFRWLMNENAMATHKLAE
GIRLFTKDTIELENIIKQNL
3D structure
PDB3tno Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.
ChainA
Resolution1.65 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) D18 E99 K135 T159 F181
Catalytic site (residue number reindexed from 1) D17 E98 K134 T158 F180
Enzyme Commision number 2.2.1.2: transaldolase.
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 I22 A D18 N36 K135 S179 F181 R184 S230 R232 D17 N35 K134 S178 F180 R183 S229 R231
Gene Ontology
Molecular Function
GO:0004801 transaldolase activity
GO:0016740 transferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006098 pentose-phosphate shunt
GO:0009052 pentose-phosphate shunt, non-oxidative branch
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3tno, PDBe:3tno, PDBj:3tno
PDBsum3tno
PubMed24531488
UniProtQ5NFX0

[Back to BioLiP]