Structure of PDB 4qg6 Chain C Binding Site BS01
Receptor Information
>4qg6 Chain C (length=406) Species:
9606
(Homo sapiens) [
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DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVAR
LNFSHGTHEYHAETIKNVRTATESFASDPILERPVAVALDTKGPAVSEKD
IQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHE
GVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVI
CATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAV
RMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCS
GAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCK
DPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTM
RVVPVP
Ligand information
Ligand ID
PRO
InChI
InChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
InChIKey
ONIBWKKTOPOVIA-BYPYZUCNSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C1C[C@H](NC1)C(=O)O
CACTVS 3.341
OC(=O)[C@@H]1CCCN1
CACTVS 3.341
OC(=O)[CH]1CCCN1
OpenEye OEToolkits 1.5.0
C1CC(NC1)C(=O)O
ACDLabs 10.04
O=C(O)C1NCCC1
Formula
C5 H9 N O2
Name
PROLINE
ChEMBL
CHEMBL54922
DrugBank
DB00172
ZINC
ZINC000000895360
PDB chain
4qg6 Chain C Residue 1001 [
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Receptor-Ligand Complex Structure
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PDB
4qg6
Structural insight into mechanisms for dynamic regulation of PKM2.
Resolution
3.207 Å
Binding residue
(original residue number in PDB)
N44 N70 H464 I469 F470
Binding residue
(residue number reindexed from 1)
N21 N47 H339 I344 F345
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R73 K270 T328
Catalytic site (residue number reindexed from 1)
R50 K145 T203
Enzyme Commision number
2.7.10.2
: non-specific protein-tyrosine kinase.
2.7.11.1
: non-specific serine/threonine protein kinase.
2.7.1.40
: pyruvate kinase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0003723
RNA binding
GO:0003729
mRNA binding
GO:0003824
catalytic activity
GO:0004713
protein tyrosine kinase activity
GO:0004743
pyruvate kinase activity
GO:0005515
protein binding
GO:0005524
ATP binding
GO:0016301
kinase activity
GO:0023026
MHC class II protein complex binding
GO:0030955
potassium ion binding
GO:0045296
cadherin binding
GO:0046872
metal ion binding
Biological Process
GO:0006096
glycolytic process
GO:0006417
regulation of translation
GO:0012501
programmed cell death
GO:0016310
phosphorylation
GO:0032869
cellular response to insulin stimulus
GO:0061621
canonical glycolysis
GO:1903672
positive regulation of sprouting angiogenesis
GO:2000767
positive regulation of cytoplasmic translation
Cellular Component
GO:0005576
extracellular region
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0005739
mitochondrion
GO:0005791
rough endoplasmic reticulum
GO:0005829
cytosol
GO:0005929
cilium
GO:0031982
vesicle
GO:0034774
secretory granule lumen
GO:0062023
collagen-containing extracellular matrix
GO:0070062
extracellular exosome
GO:1903561
extracellular vesicle
GO:1904813
ficolin-1-rich granule lumen
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:4qg6
,
PDBe:4qg6
,
PDBj:4qg6
PDBsum
4qg6
PubMed
25645022
UniProt
P14618
|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)
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