Structure of PDB 6a8p Chain A Binding Site BS01

Receptor Information
>6a8p Chain A (length=681) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNY
EASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTL
SLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYL
DSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVN
PKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVS
PMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTN
YNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPG
YEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNAD
VVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSS
EEREAFTRANHLNTGMAMRIRVGQSMNMGSDFDVFAHITNNTAEEYVCRL
LLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTE
SNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEV
SLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPL
HMGLHKLVVNFESDKLKAVKGFRNVIIGPAL
Ligand information
Ligand IDGTP
InChIInChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyXKMLYUALXHKNFT-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O14 P3
NameGUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL1233147
DrugBankDB04137
ZINCZINC000060094177
PDB chain6a8p Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6a8p Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity.
Resolution2.537 Å
Binding residue
(original residue number in PDB)		F174 R478 V479 Q481 S482 M483 R580 L582 Y583
Binding residue
(residue number reindexed from 1)		F174 R471 V472 Q474 S475 M476 R573 L575 Y576
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W241 C277 H335 D358 Y516
Catalytic site (residue number reindexed from 1) W241 C277 H335 D358 Y509
Enzyme Commision number 2.3.1.-
2.3.2.13: protein-glutamine gamma-glutamyltransferase.
3.4.-.-
3.5.1.44: protein-glutamine glutaminase.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6a8p, PDBe:6a8p, PDBj:6a8p
PDBsum6a8p
PubMed30321187
UniProtP21980|TGM2_HUMAN Protein-glutamine gamma-glutamyltransferase 2 (Gene Name=TGM2)

[Back to BioLiP]