Structure of PDB 6ltd Chain B

Receptor sequence
>6ltdB (length=882) Species: 630397 (Streptomyces sp. Sp080513GE-23) [Search protein sequence]
AAELPPLVPEPGDAGQPFPLTPTQQALWVGRACYGYFEWERPELDLARYR
RAWERLVAHHPGLRTVVRPDGTQHVLERPGPVPITVEDLRQDPDAVRRLE
ESRLDPGTWPMFDLRVVLLSGRVRVQLGIDLQLMDASSLFLNLFSDLVTL
YDDPDAALASQKLAFRDFARWLEEDVRGGARWRADWAYWQERLDGLPPAP
DLPAARKFERCMVRCPAEEFALLRERALAHGLTETELLVGAFAEVLRGWS
SDPAFTLNVPVFQRFDVPGIEDVIGDYTNPILLEARPEGRTVAERIVALA
ARLRADTRHASVNGVEVLRELARRRGLAAAAMPVVVTSLLGLPSAARSIT
EFGTEVHSITQTPQVSLDFQIRPEDGELRLVWDHRSGAFAPGVVEGAFEA
FLDLVGRMLADEPGHGVWEAPFADMRSRRDRAVWNETNDTAEPVPAVLLQ
ERFFAQARRTPDAEAVVASGLRLTYDELARHAYRIGNTLRERGVRPGDLV
GVVMEKGWEQYAAVYGILAAGGAYLPIDAASPRGRVARLLESAGAGIVLT
QSRLRDELDLPAGTTVLRADTDFETASTAPLTPVQGPDDPAYVIYTGEPK
GVVVAHRGVANLVRDVRRRFAVTPADRLLALSGLHFDASVYDVFGPLACG
ATVVVPPPFRRAEPDVWAELVRDERVTFWNSVPVLLELLVGEAESRDDRP
LATLRLAVVSGDWIPLDLPGRARAQAPGLRVVGSGGPTETICWSLFHPID
AVDPQWTSIPYGKPIANQRYYIVDRDLRPRPTWARGEMAVASPLGLALGY
LNDPERTAAKFVTLPGTGERAYLTGDFGRLLPDGGIEILGREDFQRIELG
EIGVRAAADVVIRLLPELPLTANGKVDRLALA
3D structure
PDB6ltd Structural and Functional Analyses of the Tridomain-Nonribosomal Peptide Synthetase FmoA3 for 4-Methyloxazoline Ring Formation.
ChainB
Resolution4.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T642 L662 T788 E789 R902 K982
Catalytic site (residue number reindexed from 1) T596 L612 T738 E739 R846 K875
Enzyme Commision number ?
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 AMP B G761 D762 P787 T788 E789 D876 I888 R891 G711 D712 P737 T738 E739 D826 I838 R841
BS02 EW6 B F686 G785 G786 P787 T788 F636 G735 G736 P737 T738
Gene Ontology
Molecular Function
GO:0000036 acyl carrier activity
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0031177 phosphopantetheine binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0008610 lipid biosynthetic process
GO:0017000 antibiotic biosynthetic process
GO:0043041 amino acid activation for nonribosomal peptide biosynthetic process
GO:0044550 secondary metabolite biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6ltd, PDBe:6ltd, PDBj:6ltd
PDBsum6ltd
PubMed33783097
UniProtA0A077JG85

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