Structure of PDB 7js5 Chain A

Receptor sequence
>7js5A (length=494) Species: 1890 (Streptomyces antibioticus) [Search protein sequence]
PPTPHLDAIERSLRDTSPGLEGSVWQRTDGNRLDAPDGDPAGWLLQTPGC
WGDAGCKDRAGTRRLLDKMTRNIADARHTVDISSLAPFPNGGFEDAVVDG
LKASVAAGHSPRVRILVGAAPIYHLNVVPSRYRDELIGKLGAAAGKVTLN
VASMTTSKTSLSWNASKLLVVDGKTAITGGINTNKDDYLDTAHPVSDVDM
ALSGPAARSAGKYLDTLWDWTCRNASDPAKVWLATSNGASCMPSMEQDEA
GSAPAEPTGDVPVIAVGGLGVGIKESDPSSGYHPDLPTAPDTKCTVGLHD
NTNADRDYDTVNPEENALRSLIASARSHVEISQQDLNATCPPLPRYDIRT
YDTLAGKLAAGVKVRIVVSDPANARSQIKSLDEISDTLRTRLVALTGDNE
KASRALCGNLQLASFRSSDAAKWADGKPYALHHKLVSVDDSAFYIGSKNL
YPAWLQDFGYIVESPAAAQQLKTELLDPEWKYSQQAAATPAGCP
3D structure
PDB7js5 Structures of an engineered phospholipase D with specificity for secondary alcohol transphosphatidylation: insights into plasticity of substrate binding and activation.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.4.4: phospholipase D.
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 IPD A L88 K170 Q337 H442 K444 N459 Y461 L85 K167 Q334 H432 K434 N449 Y451
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004630 phospholipase D activity
GO:0016787 hydrolase activity
GO:0030572 phosphatidyltransferase activity
Biological Process
GO:0016042 lipid catabolic process
GO:0032049 cardiolipin biosynthetic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7js5, PDBe:7js5, PDBj:7js5
PDBsum7js5
PubMed33843991
UniProtQ53728|PLD_STRAT Phospholipase D

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