Structure of PDB 2ozl Chain B

Receptor sequence

>2ozlB (length=330) Species: 9606 (Homo sapiens)

SLQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGD
KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAK
TYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWN
SEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAK
IERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETI
EASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGAD
VPMPYAKILEDNSIPQVKDIIFAIKKTLNI

3D structure

• PDB: 2ozl Phosphorylation of Serine 264 Impedes Active Site Accessibility in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E59 H128
• Catalytic site (residue number reindexed from 1): E60 H129
• 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	B	E28 I57 E59 F85 Q88	E29 I58 E60 F86 Q89

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:2ozl, PDBe:2ozl, PDBj:2ozl
• PDBsum: 2ozl
• PubMed: 17474719
• UniProt: P11177|ODPB_HUMAN Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (Gene Name=PDHB)