Structure of PDB 3tk7 Chain A

Receptor sequence
>3tk7A (length=320) Species: 119856 (Francisella tularensis subsp. tularensis) [Search protein sequence]
QKSVLEQLKQVTMVVADTGDFELIKKYKPVDATTNPSLILKAVKEQKYSN
LVAETISKVKANNPDLNSDDLVKEIAIEILVSFGIKILDVIEGKVSSEVD
ARVSFNSATTIDYAKRIIARYESNGIPKDRVLIKIAATWEGIKAAKLLQK
EGINCNLTLIFDKAQAKACAEAGVYLVSPFVGRITDWQMQQNNLKTFPAI
ADDDGVNSVKAIYKLYKSHGFKTIVMGASFRNVEQVIALAGCDALTISPV
LLEELKNRDEHLEVKLTKNDDVVTQSPQISEADFRWLMNENAMATHKLAE
GIRLFTKDTIELENIIKQNL
3D structure
PDB3tk7 Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 F6R 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tk7, PDBe:3tk7, PDBj:3tk7
PDBsum3tk7
PubMed24531488
UniProtQ5NFX0

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