Structure of PDB 1kv3 Chain A

Receptor sequence
>1kv3A (length=651) Species: 9606 (Homo sapiens) [Search protein sequence]
ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPAPSQEAGTKAR
FPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASGHFI
LLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFQ
DGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV
LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACT
VLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHC
WVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLST
KYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER
EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVGQSMNMG
SDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLTLEP
FSEKSVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLEN
PEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV
EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAVKGFRNVIIGP
A
3D structure
PDB1kv3 Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W241 C277 H335 D358 Y516
Catalytic site (residue number reindexed from 1) W205 C241 H299 D322 Y480
Enzyme Commision number 2.3.1.-
2.3.2.13: protein-glutamine gamma-glutamyltransferase.
3.4.-.-
3.5.1.44: protein-glutamine glutaminase.
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 GDP A F174 R478 V479 G480 Q481 S482 M483 R580 L582 Y583 F138 R442 V443 G444 Q445 S446 M447 R544 L546 Y547
Gene Ontology
Molecular Function
GO:0003810 protein-glutamine gamma-glutamyltransferase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0008233 peptidase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
GO:0050568 protein-glutamine glutaminase activity
GO:0120294 peptide serotonyltransferase activity
GO:0120295 histone serotonyltransferase activity
GO:0120296 peptide dopaminyltransferase activity
GO:0120297 histone dopaminyltransferase activity
GO:0120298 peptide noradrenalinyltransferase activity
GO:0120299 peptide histaminyltransferase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006508 proteolysis
GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway
GO:0010467 gene expression
GO:0014046 dopamine secretion
GO:0018149 peptide cross-linking
GO:0018277 protein deamination
GO:0032471 negative regulation of endoplasmic reticulum calcium ion concentration
GO:0042981 regulation of apoptotic process
GO:0043065 positive regulation of apoptotic process
GO:0043277 apoptotic cell clearance
GO:0043547 positive regulation of GTPase activity
GO:0045785 positive regulation of cell adhesion
GO:0050769 positive regulation of neurogenesis
GO:0051057 positive regulation of small GTPase mediated signal transduction
GO:0051561 positive regulation of mitochondrial calcium ion concentration
GO:0060348 bone development
GO:0060445 branching involved in salivary gland morphogenesis
GO:0060662 salivary gland cavitation
GO:0071314 cellular response to cocaine
GO:1903351 cellular response to dopamine
GO:1903672 positive regulation of sprouting angiogenesis
GO:1904015 cellular response to serotonin
GO:2000425 regulation of apoptotic cell clearance
Cellular Component
GO:0000785 chromatin
GO:0000786 nucleosome
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005925 focal adhesion
GO:0031012 extracellular matrix
GO:0048471 perinuclear region of cytoplasm
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kv3, PDBe:1kv3, PDBj:1kv3
PDBsum1kv3
PubMed11867708
UniProtP21980|TGM2_HUMAN Protein-glutamine gamma-glutamyltransferase 2 (Gene Name=TGM2)

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