Structure of PDB 2a8j Chain A

Receptor sequence
>2a8jA (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
GGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAAL
VELEDSPFTNAGMGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPV
SVANRLLCEGQKGKLGRIPPCFLVGEGAYRWAVDHGIPSCPTVGAVVVDH
EGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSG
CGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSPFLASEDGVLGG
VIVLRSCLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAVAGQSV
AIEGGVCRLE
3D structure
PDB2a8j Crystal Structure of Human Taspase1, a Crucial Protease Regulating the Function of MLL.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N100
Catalytic site (residue number reindexed from 1) N60
Enzyme Commision number 3.4.25.-
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 CL A G49 T99 T234 G9 T59 T142
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
GO:0040029 epigenetic regulation of gene expression
GO:0045893 positive regulation of DNA-templated transcription
GO:0051604 protein maturation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2a8j, PDBe:2a8j, PDBj:2a8j
PDBsum2a8j
PubMed16216576
UniProtQ9H6P5|TASP1_HUMAN Threonine aspartase 1 (Gene Name=TASP1)

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