Structure of PDB 1v0v Chain A

Receptor sequence
>1v0vA (length=492) Species: 172564 (Streptomyces sp. PMF) [Search protein sequence]
SATPHLDAVEQTLRQVSPGLEGDVWERTSGNKLDGSAADPSDWLLQTPGC
WGDDKCADRVGTKRLLAKMTENIGNATRTVDISTLAPFPNGAFQDAIVAG
LKESAAKGNKLKVRILVGAAPVIPSKYRDELTAKLGKAAENITLNVASMT
TSKTAFSWNHSKILVVDGQSALTGGINSWKDDYLDTTHPVSDVDLALTGP
AAGSAGRYLDTLWTWTCQNKSNIASVWFAASGNAGCMPTMHKDTNPKASP
ATGNVPVIAVGGLGVGIKDVDPKSTFRPDLPTASDTKCVVGLHDNTNADR
DYDTVNPEESALRALVASAKGHIEISQQDLNATCPPLPRYDIRLYDALAA
KMAAGVKVRIVVSDPANRGYSQIKSLSEISDTLRNRLANITGGQQAAKTA
MCSNLQLATFRSSPNGKWADGHPYAQHHKLVSVDSSTFYIGSKNLYPSWL
QDFGYIVESPEAAKQLDAKLLDPQWKYSQETATVDYARGICN
3D structure
PDB1v0v The Reaction Mechanism of Phospholipase D from Streptomyces Sp. Strain Pmf. Snapshots Along the Reaction Pathway Reveal a Pentacoordinate Reaction Intermediate and an Unexpected Final Product
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H170 D202 H448 D473
Catalytic site (residue number reindexed from 1) H160 D192 H427 D452
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 PO3 A H170 K172 H448 K450 H160 K162 H427 K429
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004630 phospholipase D activity
GO:0030572 phosphatidyltransferase activity
Biological Process
GO:0032049 cardiolipin biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1v0v, PDBe:1v0v, PDBj:1v0v
PDBsum1v0v
PubMed15165852
UniProtP84147

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