Structure of PDB 5n9x Chain A

Receptor sequence
>5n9xA (length=489) Species: 1931 (Streptomyces sp.) [Search protein sequence]
GATLVDLFSRAAMEMPDRTALHIDDEKISYGLLHSWAEGLADLLHDAGVR
KGDRVALRMPPGANAIAAMLGILRAGAAYVPLDIRNPPARNAFIVTDSQV
VALVGDPIPEYTGPLVTEENVAALRPGPERPGPQDVAYIIYTSGTTGRPK
GVPVRHGNVTALFEACSRLFSFSADDRWLLFHSMAFDFSVWEIWGALSTG
AELVVLPYWTARTPVETARVVRDRGITVLNQTPTAFGALTTAVLGEGIDL
PELRYVVFGGEKLTPAVVRPWAKRFGLDRPHLINMYGITETTVHATFHRL
TEDDLAAEDSVIGRPLPGFTHRIVTEDGRDAATGEPGELWLAGPQVSEGY
LNRPELTAERFTTGPPPRYYHSGDLVSRRAGGDLVYQGRADLQVKLRGHR
IELSDVEAAVRTHPAVVDAVVWVHEFAPGDSRLVCAYTAPDARALRAHVK
TVLPSYMQPSQYLALPELPRTINGKADRASVARAFDERR
3D structure
PDB5n9x Structure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity.
ChainA
Resolution2.396 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T167 L187 T314 E315 K427 R432 K515
Catalytic site (residue number reindexed from 1) T142 L162 T289 E290 K395 R400 K475
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 THR A F211 D212 F213 G285 G312 V318 K515 F186 D187 F188 G260 G287 V293 K475
BS02 ATP A T167 S168 K175 G285 E286 K287 N309 M310 Y311 G312 I313 T314 D406 Y418 R421 K515 T142 S143 K150 G260 E261 K262 N284 M285 Y286 G287 I288 T289 D374 Y386 R389 K475
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0031177 phosphopantetheine binding
Biological 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:5n9x, PDBe:5n9x, PDBj:5n9x
PDBsum5n9x
PubMed28704585
UniProtH6SG27

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