Structure of PDB 6i2r Chain C

Receptor sequence
>6i2rC (length=822) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
DSIEDKNARVIELIAAYRNRGHLMADIDPLRLDNTRFLTLWDLDREFKVV
QRKKLRDILSVLRDAYCRHVGVEYTHILEPEQQRWIQERVETKHDKPTVA
EQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAVIDQCAE
HGLDEVVIAMPHRGRLNVLANIVGKPYSQIFSEFEGDVKYHLGATGTYIQ
MFGDNDIEVSLTANPSHLEAVDPVLEGLVRAKQDLLDTGEEGSDNRFSVV
PLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHIVVNNQIGFTTAPTD
SRSSEYCTDVAKMIGAPIFHVNGDDPEACAWVARLAVDFRQAFKKDVVID
MLCYRRRGHNEGDDPSMTQPYMYDVIDTKRGSRKAYTEALIGRGDISMKE
AEDALRDYQGQLEAVFNEVRELEKHLATAVDKAMLQRIGDAHLALPEGFT
VHPRVRPVLEKRREMAYEGRIDWAFAELLALGSLIAEGKLVRLSGQDTQR
GTFTQRHAVIVDRKTGEEFTPLQLLATNPDGTPTGGKFLVYNSALSEFAA
VGFEYGYSVGNPDAMVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDV
VLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIAMPSTPANYFHLLRRH
GKDGIQRPLIVFTPKSMLRNKAAVSDIRDFTESKFRSVLEEPMYTDGEGD
RNKVTRLLLTSGKIYYELAARKAKENREDVAIVRIEQLAPLPRRRLAETL
DRYPNVKEKFWVQEEPANQGAWPSFGLTLPEILPDHFTGLKRISRRAMSA
PSSGSSKVHAVEQQEILDTAFG
3D structure
PDB6i2r Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling.
ChainC
Resolution2.2 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 1.2.4.2: oxoglutarate dehydrogenase (succinyl-transferring).
2.2.1.5: 2-hydroxy-3-oxoadipate synthase.
2.3.1.61: dihydrolipoyllysine-residue succinyltransferase.
4.1.1.71: 2-oxoglutarate decarboxylase.
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 TPP C Q901 L950 E952 Q976 F980 Q496 L545 E547 Q571 F575
BS02 TPP C R540 S604 L606 G644 D645 A646 A647 N678 I680 H747 R163 S216 L218 G256 D257 A258 A259 N290 I292 H359
BS03 MG C D645 N678 I680 D257 N290 I292
BS04 CA C D1004 H1055 D1058 I1060 D599 H650 D653 I655
Gene Ontology
Molecular Function
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
GO:0030976 thiamine pyrophosphate binding

View graph for
Molecular Function
External links
PDB RCSB:6i2r, PDBe:6i2r, PDBj:6i2r
PDBsum6i2r
PubMed31064884
UniProtA0R2B1|KGD_MYCS2 Multifunctional 2-oxoglutarate metabolism enzyme (Gene Name=kgd)

[Back to BioLiP]