Structure of PDB 1fc4 Chain A

Receptor sequence
>1fc4A (length=401) Species: 562 (Escherichia coli) [Search protein sequence]
GSHMRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINF
CANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLA
AFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCK
AKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVC
DLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALG
GASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSE
LRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQK
EGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVI
A
3D structure
PDB1fc4 Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AKB A N50 H136 S185 H213 K244 R368 N53 H139 S188 H216 K247 R371
BS02 PLP A S110 C111 F112 H136 S185 D210 S212 H213 T241 K244 S113 C114 F115 H139 S188 D213 S215 H216 T244 K247
BS03 PLP A F273 S274 N275 F276 S277 N278
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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