Structure of PDB 7bxq Chain B

Receptor sequence
>7bxqB (length=399) Species: 106590 (Cupriavidus necator) [Search protein sequence]
MSNAEAFYASIRTELESIRAAGLFKNERVIATPQGARVRTTDGREVINLC
ANNYLGLSSHPQVIEAAHEALRTHGFGLSSVRFICGTQDLHKTLEARLSA
FLGTEDTILYGSAFDANGGLFETLLGAEDAVISDALNHASIIDGVRLSKA
RRYRYQHNDMDDLRVQLEQARADGARYTLVFSDGVFSMDGTVARLDEMRA
ICDEYGALLGIDECHATGFMGQRGRGTHEARGVFGKIDIITGTLGAALGG
ASGGFTSARKEVVALLRQRSRPYLFSNTVAPAIVGASIAVLDILEASTEL
RDRLEGNTRFFRAGLDRLGFDVKAGDHPIIPIMVYDADKAQQLAQRLLEL
GVYVVGFFYPVVPKGQARIRVQMSALHDEAALQAALDAFGQAGRELGLI
3D structure
PDB7bxq Chemoenzymatic synthesis of 3-ethyl-2,5-dimethylpyrazine by L-threonine 3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase/L-threonine aldolase
ChainB
Resolution2.49 Å
3D
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Enzymatic activity
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 2BK B V81 F275 S276 N277 V81 F275 S276 N277
BS02 2BK B A113 F114 H138 S187 M188 D212 C214 H215 T243 R370 A113 F114 H138 S187 M188 D212 C214 H215 T243 R370
Gene Ontology
Molecular Function
GO:0008890 glycine C-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016874 ligase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006567 threonine catabolic process
GO:0009058 biosynthetic process
GO:0019518 L-threonine catabolic process to glycine
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:7bxq, PDBe:7bxq, PDBj:7bxq
PDBsum7bxq
PubMed
UniProtQ0K313

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