Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 1xva Chain B Binding Site BS01

Receptor Information
>1xva Chain B (length=292) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLG
LLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWN
RRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQ
SEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTK
DITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASF
TELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG
Ligand information
Ligand IDACT
InChIInChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKeyQTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04[O-]C(=O)C
OpenEye OEToolkits 1.5.0CC(=O)[O-]
CACTVS 3.341CC([O-])=O
FormulaC2 H3 O2
NameACETATE ION
ChEMBL
DrugBankDB14511
ZINC
PDB chain1xva Chain B Residue 294 [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]
PDB1xva Crystal structure of glycine N-methyltransferase from rat liver.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		W30 I34 L240
Binding residue
(residue number reindexed from 1)		W30 I34 L240
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y21 G137 H142 R175 Y194
Catalytic site (residue number reindexed from 1) Y21 G137 H142 R175 Y194
Enzyme Commision number 2.1.1.20: glycine N-methyltransferase.
Gene Ontology
Molecular Function
GO:0005542 folic acid binding
GO:0008168 methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016594 glycine binding
GO:0017174 glycine N-methyltransferase activity
GO:0042802 identical protein binding
GO:0098603 selenol Se-methyltransferase activity
GO:1904047 S-adenosyl-L-methionine binding
Biological Process
GO:0005977 glycogen metabolic process
GO:0006111 regulation of gluconeogenesis
GO:0006544 glycine metabolic process
GO:0006555 methionine metabolic process
GO:0006730 one-carbon metabolic process
GO:0032259 methylation
GO:0046498 S-adenosylhomocysteine metabolic process
GO:0046500 S-adenosylmethionine metabolic process
GO:0051289 protein homotetramerization
GO:1901052 sarcosine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034708 methyltransferase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1xva, PDBe:1xva, PDBj:1xva
PDBsum1xva
PubMed8810903
UniProtP13255|GNMT_RAT Glycine N-methyltransferase (Gene Name=Gnmt)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417