Structure of PDB 6aj6 Chain C

Receptor sequence
>6aj6C (length=413) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SNKISATGVLVELDGDEMTRVIWKKIKETLIFPFVNVPIEYYDLSMENRD
KTEDRVTVEAAYAIKKHGVGVKCATITPDEARVKEFNLKKMWRSPNGTIR
TILGGTVFREPIICSNVPRLVTTWKKPVVIGRHAFGDQYSATDAVVKEPG
TFEMRFIPANGGEPKVYKVFDYKSGGVMMGMYNTDDSIRDFARSCFEFAL
ARKWPLYLSTKNTILKHYDGRFKDIFAEMYKALYETKFKTCGIFYEHRLI
DDMVAHCMRSEGGYVWACKNYDGDVQSDSLAQGFGSLGMMTSILMTPDGK
TVEVEAAHGTVTRHYRDYQKGKETSTNPVASIFAWTRALAHRARVDNNNT
LLEFTQRLEDVIIATIEAGAMTEDLAICIKGEKNVVRADYLNTDEFIDAV
SQRLKVAMQKSKV
3D structure
PDB6aj6 Biochemical characterization of a novel Trypanosoma brucei glycosomal isocitrate dehydrogenase with dual coenzyme specificity (NADP+/NAD+)
ChainC
Resolution3.2 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 1.1.1.42: isocitrate dehydrogenase (NADP(+)).
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 NAP C T75 I76 T77 R82 L287 H308 G309 T310 V311 R313 H314 T326 N327 T75 I76 T77 R82 L287 H308 G309 T310 V311 R313 H314 T326 N327
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006102 isocitrate metabolic process
GO:0006739 NADP metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0020015 glycosome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6aj6, PDBe:6aj6, PDBj:6aj6
PDBsum6aj6
PubMed
UniProtQ387G0

[Back to BioLiP]