Structure of PDB 3tjv Chain A

Receptor sequence
>3tjvA (length=225) Species: 9606 (Homo sapiens) [Search protein sequence]
IIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHCQGSSI
NVTLGAHNIKEQERTQQFIPVKRPIPHPAYNPKNFSNNIMLLQLERKAKW
TTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDC
QCERLFHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQGILSYGN
KKGTPPGVYIKVSHFLPWIKRTMKR
3D structure
PDB3tjv Structural insights into the substrate specificity of human granzyme H: the functional roles of a novel RKR motif
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H59 N103 K194 G195 D196 S197 G198
Catalytic site (residue number reindexed from 1) H44 N88 K179 G180 D181 S182 G183
Enzyme Commision number 3.4.21.-
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 peptide A Q34 R41 K42 R43 C44 H59 F100 N174 F193 K194 G195 S197 Y213 G214 N215 K216 Q19 R26 K27 R28 C29 H44 F85 N159 F178 K179 G180 S182 Y198 G199 N200 K201
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006915 apoptotic process
GO:0031640 killing of cells of another organism
Cellular Component
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle
GO:0044194 cytolytic granule

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tjv, PDBe:3tjv, PDBj:3tjv
PDBsum3tjv
PubMed22156497
UniProtP20718|GRAH_HUMAN Granzyme H (Gene Name=GZMH)

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