Structure of PDB 9bc3 Chain A Binding Site BS01
Receptor Information
>9bc3 Chain A (length=431) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNY
EASVDSLTFSVVTGPAPSQEAGTKARFPLRDWTATVVDQQDCTLSLQLTT
PANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEER
QEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKN
AGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVSPMSWIG
SVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHD
QNSNLLIEYFRSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSE
GTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSI
NRSLIVGLKISTKSVGRDEREDITHTYKYPE
Ligand information
>9bc3 Chain C (length=5) Species:
32630
(synthetic construct) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
PKLPF
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
9bc3
Structural and mechanistic analysis of Ca 2+ -dependent regulation of transglutaminase 2 activity using a Ca 2+ -bound intermediate state.
Resolution
2.52 Å
Binding residue
(original residue number in PDB)
Q169 W241 M252 C277 W278 N302 I331 W332 N333 F334 H335 Q362 L420
Binding residue
(residue number reindexed from 1)
Q163 W235 M246 C271 W272 N296 I315 W316 N317 F318 H319 Q346 L404
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:9bc3
,
PDBe:9bc3
,
PDBj:9bc3
PDBsum
9bc3
PubMed
38959038
UniProt
P21980
|TGM2_HUMAN Protein-glutamine gamma-glutamyltransferase 2 (Gene Name=TGM2)
[
Back to BioLiP
]