Structure of PDB 1fc4 Chain B Binding Site BS03

Receptor Information
>1fc4 Chain B (length=401) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSHMRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINF
CANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLA
AFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCK
AKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVC
DLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALG
GASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSE
LRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQK
EGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVI
A
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1fc4 Chain B Residue 1203 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1fc4 Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		S110 C111 F112 H136 D181 S185 D210 S212 H213 T241 K244
Binding residue
(residue number reindexed from 1)		S113 C114 F115 H139 D184 S188 D213 S215 H216 T244 K247
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N50 H136 D181 S185 D210 H213 K244
Catalytic site (residue number reindexed from 1) N53 H139 D184 S188 D213 H216 K247
Enzyme Commision number 2.3.1.29: glycine C-acetyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008890 glycine C-acetyltransferase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016874 ligase activity
GO:0030170 pyridoxal phosphate binding
GO:0046872 metal ion binding
Biological Process
GO:0006567 threonine catabolic process
GO:0009058 biosynthetic process
GO:0019518 L-threonine catabolic process to glycine
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fc4, PDBe:1fc4, PDBj:1fc4
PDBsum1fc4
PubMed11318637
UniProtP0AB77|KBL_ECOLI 2-amino-3-ketobutyrate coenzyme A ligase (Gene Name=kbl)

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