Structure of PDB 5n9x Chain A Binding Site BS01

Receptor Information
>5n9x Chain A (length=489) Species: 1931 (Streptomyces sp.) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GATLVDLFSRAAMEMPDRTALHIDDEKISYGLLHSWAEGLADLLHDAGVR
KGDRVALRMPPGANAIAAMLGILRAGAAYVPLDIRNPPARNAFIVTDSQV
VALVGDPIPEYTGPLVTEENVAALRPGPERPGPQDVAYIIYTSGTTGRPK
GVPVRHGNVTALFEACSRLFSFSADDRWLLFHSMAFDFSVWEIWGALSTG
AELVVLPYWTARTPVETARVVRDRGITVLNQTPTAFGALTTAVLGEGIDL
PELRYVVFGGEKLTPAVVRPWAKRFGLDRPHLINMYGITETTVHATFHRL
TEDDLAAEDSVIGRPLPGFTHRIVTEDGRDAATGEPGELWLAGPQVSEGY
LNRPELTAERFTTGPPPRYYHSGDLVSRRAGGDLVYQGRADLQVKLRGHR
IELSDVEAAVRTHPAVVDAVVWVHEFAPGDSRLVCAYTAPDARALRAHVK
TVLPSYMQPSQYLALPELPRTINGKADRASVARAFDERR
Ligand information
Ligand IDTHR
InChIInChI=1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1
InChIKeyAYFVYJQAPQTCCC-GBXIJSLDSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(N)C(O)C
OpenEye OEToolkits 1.5.0CC(C(C(=O)O)N)O
CACTVS 3.341C[CH](O)[CH](N)C(O)=O
CACTVS 3.341C[C@@H](O)[C@H](N)C(O)=O
OpenEye OEToolkits 1.5.0C[C@H]([C@@H](C(=O)O)N)O
FormulaC4 H9 N O3
NameTHREONINE
ChEMBLCHEMBL291747
DrugBankDB00156
ZINCZINC000000895103
PDB chain5n9x Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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.
Resolution2.396 Å
Binding residue
(original residue number in PDB)		F211 D212 F213 G285 G312 V318 K515
Binding residue
(residue number reindexed from 1)		F186 D187 F188 G260 G287 V293 K475
Annotation score4
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 ?
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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