Structure of PDB 2yic Chain B

Receptor sequence
>2yicB (length=810) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
DKNARVIELIAAYRNRGHLMADIDPLRLDNTRFWDLDREFKRKKLRDILS
VLRDAYCRHVGVEYTHILEPEQQRWIQERVETKHDKPTVAEQKYILSKLN
AAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAVIDQCAEHGLDEVVIAM
PHRGRLNVLANIVGKPYSQIFSEFDVKYHLGATGTYIQMFGDNDIEVSLT
ANPSHLEAVDPVLEGLVRAKQDLLDTGEEGSDNRFSVVPLMLHGDAAFAG
QGVVAETLNLALLRGYRTGGTIHIVVNNQIGFTTAPTDSRSSEYCTDVAK
MIGAPIFHVNGDDPEACAWVARLAVDFRQAFKKDVVIDMLCYRRRGHNEG
DDPSMTQPYMYDVIDTKRGSRKAYTEALIGRGDISMKEAEDALRDYQGQL
ERVFNEVRELEKHLATAVDKAMLQRIGDAHLALPEGFTVHPRVRPVLEKR
REMAYEGRIDWAFAELLALGSLIAEGKLVRLSGQDTQRGTFTQRHAVIVD
RKTGEEFTPLQLLATNPDGTPTGGKFLVYNSALSEFAAVGFEYGYSVGNP
DAMVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQG
PDHTSGRIERFLQLWAEGSMTIAMPSTPANYFHLLRRHGKDGIQRPLIVF
TPKSMLRNKAAVSDIRDFTESKFRSVLEEPMYTDGEGDRNKVTRLLLTSG
KIYYELAARKAKENREDVAIVRIEQLAPLPRRRLAETLDRYPNVKEKFWV
QEEPANQGAWPSFGLTLPEILPDHFTGLKRISRRAMSAPSSGSSKVHAVE
QQEILDTAFG
3D structure
PDB2yic Functional Plasticity and Allosteric Regulation of Alpha-Ketoglutarate Decarboxylase in Central Mycobacterial Metabolism.
ChainB
Resolution1.96 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 B Q901 L950 E952 Q976 F980 Q484 L533 E535 Q559 F563
BS02 TPP B R540 S604 L606 G644 D645 A646 A647 N678 I680 G681 H747 R153 S204 L206 G244 D245 A246 A247 N278 I280 G281 H347
BS03 MG B D645 N678 I680 D245 N278 I280
BS04 CA B D1004 H1055 D1058 I1060 D587 H638 D641 I643
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:2yic, PDBe:2yic, PDBj:2yic
PDBsum2yic
PubMed21867916
UniProtA0R2B1|KGD_MYCS2 Multifunctional 2-oxoglutarate metabolism enzyme (Gene Name=kgd)

[Back to BioLiP]