Structure of PDB 3exh Chain H

Receptor sequence

>3exhH (length=329) Species: 9606 (Homo sapiens)

LQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDK
RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKT
YYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS
EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKI
ERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIE
ASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADV
PMPYAKILEDNSIPQVKDIIFAIKKTLNI

3D structure

• PDB: 3exh Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
• Chain: H
• Resolution: 2.444 Å

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	H	I57 E59 F85 Q88	I57 E59 F85 Q88

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

External links

• PDB: RCSB:3exh, PDBe:3exh, PDBj:3exh
• PDBsum: 3exh
• PubMed: 19081061
• UniProt: P11177|ODPB_HUMAN Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (Gene Name=PDHB)