Structure of PDB 2xt6 Chain B

Receptor sequence
>2xt6B (length=989) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
VRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLLGYAIVQTNLGLAVVAA
IKRCETMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTIGAGAMESE
ERIADLGIGKLITLTSGAESGDFLRTIHQLLLDDDFFDEIFRELGIPYEP
VRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDNTRFRSHPD
LDVNSHGLTLWDLDREFKVDGFAGVQRKKLRDILSVLRDAYCRHVGVEYT
HILEPEQQRWIQERVETKHDKPTVAEQKYILSKLNAAEAFETFLQTKYVG
QKRFSLEGAETVIPMMDAVIDQCAEHGLDEVVIAMPHRGRLNVLANIVGK
PYSQIFSDVKYHLGATGTYIQMFGDNDIEVSLTANPSHLEAVDPVLEGLV
RAKQDLLDTGEEGSDNRFSVVPLMLHGDAAFAGQGVVAETLNLALLRGYR
TGGTIHIVVNNQIGFTTAPTDSRSSEYCTDVAKMIGAPIFHVNGDDPEAC
AWVARLAVDFRQAFKKDVVIDMLCYRRRGHNEGDDPSMTQPYMYDVIDTK
RGSRKAYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELATAVDKA
MLQRIGDAHLALPEGFTVHPRVRPVLEKRREMAYEGRIDWAFAELLALGS
LIAEGKLVRLSGQDTQRGTFTQRHAVIVDRKTGEEFTPLQLLATNPDGTP
TGGKFLVYNSALSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFVNGAQSII
DEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMT
IAMPSTPANYFHLLRRHGKDGIQRPLIVFTPKSMLRNKAAVSDIRDFTES
KFRSVLEEPMYTDGEGDRNKVTRLLLTSGKIYYELAARKAKENREDVAIV
RIEQLAPLPRRRLAETLDRYPNVKEKFWVQEEPANQGAWPSFGLTLPEIL
PDHFTGLKRISRRAMSAPSSGSSKVHAVEQQEILDTAFG
3D structure
PDB2xt6 Functional Plasticity and Allosteric Regulation of Alpha-Ketoglutarate Decarboxylase in Central Mycobacterial Metabolism.
ChainB
Resolution2.74 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T256
Catalytic site (residue number reindexed from 1) T91
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 Q663 L712 E714 Q738 F742
BS02 TPP B R540 S604 H605 L606 G644 D645 A646 A647 N678 I680 H747 R338 S387 H388 L389 G427 D428 A429 A430 N461 I463 H530
BS03 MG B D645 N678 I680 D428 N461 I463
BS04 CA B D1004 H1055 D1058 I1060 D766 H817 D820 I822
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity
GO:0004591 oxoglutarate dehydrogenase (succinyl-transferring) activity
GO:0008683 2-oxoglutarate decarboxylase activity
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
GO:0016746 acyltransferase activity
GO:0016831 carboxy-lyase activity
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
GO:0050439 2-hydroxy-3-oxoadipate synthase activity
Biological Process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005829 cytosol
GO:0045252 oxoglutarate dehydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xt6, PDBe:2xt6, PDBj:2xt6
PDBsum2xt6
PubMed21867916
UniProtA0R2B1|KGD_MYCS2 Multifunctional 2-oxoglutarate metabolism enzyme (Gene Name=kgd)

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