Structure of PDB 3exh Chain D

Receptor sequence
>3exhD (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
LQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDK
RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKT
YYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS
EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKI
ERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIE
ASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADV
PMPYAKILEDNSIPQVKDIIFAIKKTLNI
3D structure
PDB3exh Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
ChainD
Resolution2.444 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E59 H128
Catalytic site (residue number reindexed from 1) E59 H128
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring).
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 D E28 I57 E59 F85 Q88 E28 I57 E59 F85 Q88 PDBbind-CN: -logKd/Ki=4.88,Kd=13.1uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0034604 pyruvate dehydrogenase (NAD+) activity
GO:0046872 metal ion binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006086 acetyl-CoA biosynthetic process from pyruvate
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0045254 pyruvate dehydrogenase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:3exh, PDBe:3exh, PDBj:3exh
PDBsum3exh
PubMed19081061
UniProtP11177|ODPB_HUMAN Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (Gene Name=PDHB)

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