Structure of PDB 6rng Chain B

Receptor sequence
>6rngB (length=334) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
SKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRAL
RELLFTTPGALPCLSGVILFEETLYQKSSDGTPFVDMLKSAGVLPGIKVD
KGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPS
QLAIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVL
AACYKALSDHHVLLEGTLLKPNMVTPGSESAKVAPEVIAEHTVRALQRTV
PAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTL
KTWGGKEENVKKAQEAFLVRCKANSEATLGAYKG
3D structure
PDB6rng Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D30 K142 E183 E185 K225 S295
Catalytic site (residue number reindexed from 1) D25 K137 E178 E180 K220 S290
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 GLY B G267 R298 G262 R293
BS02 PRO B G267 R298 G262 R293
Gene Ontology
Molecular Function
GO:0003729 mRNA binding
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0016829 lyase activity
GO:1901149 salicylic acid binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0031930 mitochondria-nucleus signaling pathway
GO:0071456 cellular response to hypoxia
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009506 plasmodesma

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Molecular Function
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Cellular Component
External links
PDB RCSB:6rng, PDBe:6rng, PDBj:6rng
PDBsum6rng
PubMed
UniProtQ9SJQ9|ALFC6_ARATH Fructose-bisphosphate aldolase 6, cytosolic (Gene Name=FBA6)

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