Structure of PDB 5kdr Chain B

Receptor sequence
>5kdrB (length=250) Species: 273036 (Staphylococcus aureus RF122) [Search protein sequence]
IMTKCPKCKKIMYTKELAENLNVCFNCDHHIALTAYKRIEAISDEGSFTE
FDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDGMKFGVAVM
DSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLM
QMGKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALI
GFAGRRVIEQTINDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEV
3D structure
PDB5kdr Crystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide B.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G207 G208
Catalytic site (residue number reindexed from 1) G179 G180
Enzyme Commision number 2.1.3.15: acetyl-CoA carboxytransferase.
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 YT5 B M134 G166 G167 T206 G207 G208 A231 G232 V235 M106 G138 G139 T178 G179 G180 A203 G204 V207 PDBbind-CN: -logKd/Ki=8.30,Ki=5nM
BS02 ZN B C33 C36 C52 C55 C5 C8 C24 C27
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5kdr, PDBe:5kdr, PDBj:5kdr
PDBsum5kdr
PubMed27471863
UniProtQ2FXM6|ACCD_STAA8 Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (Gene Name=accD)

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