Structure of PDB 6du6 Chain B

Receptor sequence
>6du6B (length=509) Species: 7159 (Aedes aegypti) [Search protein sequence]
SVSHLEHMCSLDIDSQTAFVRLSGIICTIGPASVAPEMLEKMMATGMNIA
RLNFSHGSHEYHANTIKNIREAVDNYSKKQGKPFPLAIALDTKGPEIRTG
LIEGSGTGEVELKKGEQIQLTTDKDHLEKGSKDKIFVDYVNIVKVVKKGD
RVFVDDGLISLVVDSISGDTLTCTVENGGLLGSRKGVNLPGVPVDLPAVS
EKDKSDLQFGVEQGVDVIFASFIRNAAALKEIRTILGEKGKNIKIISKIE
NQQGMQNLDAIIAASDGIMVARGDLGIEIPAEKVFLAQKSMIARCNRAGK
PVICATQMLESMIKKPRPTRAEISDVANAIIDGADCVMLSGETAKGEYPL
ECVLTMAKTCKEAEAALWHRNLFNDLVNTTPTPLDTASSIAIAASEAAAK
SRAAAVIVITTSGRSAHLISKYRPRCPIIAVTRFAQTARQCHLYRGILPV
IYEQQALEDWLKDVDARVQYGMDFGKERGFLKPGNPVVVVTGWKQGSGFT
NTIRIVNVE
3D structure
PDB6du6 Distinctive regulatory properties of pyruvate kinase 1 from Aedes aegypti mosquitoes.
ChainB
Resolution3.513 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) R71 R118 K268 T326
Catalytic site (residue number reindexed from 1) R51 R98 K248 T306
Enzyme Commision number 2.7.1.40: pyruvate kinase.
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 FBP B T430 T431 S432 S435 W480 R487 G512 K514 G516 S517 G518 F519 T410 T411 S412 S415 W460 R467 G492 K494 G496 S497 G498 F499
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004743 pyruvate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6du6, PDBe:6du6, PDBj:6du6
PDBsum6du6
PubMed30578824
UniProtQ16F38

[Back to BioLiP]