Structure of PDB 5jrh Chain B Binding Site BS03

Receptor Information
>5jrh Chain B (length=639) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KHAIPANIADRCLINPEQYETKYKQSINDPDTFWGEQGKILDWITPYQKV
KNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDTSQS
KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARI
GAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRSIPLKKNVDDA
LKNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQPEAMNA
EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTA
DVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHQVNILY
TAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKE
KCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHP
QEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRD
EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIK
GQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKT
RSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain5jrh Chain B Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5jrh Cyclic AMP Inhibits the Activity and Promotes the Acetylation of Acetyl-CoA Synthetase through Competitive Binding to the ATP/AMP Pocket.
Resolution1.644 Å
Binding residue
(original residue number in PDB)		V537 H539 I542
Binding residue
(residue number reindexed from 1)		V532 H534 I537
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T264 T416 E417 N521 R526 K609
Catalytic site (residue number reindexed from 1) T259 T411 E412 N516 R521 K604
Enzyme Commision number 6.2.1.1: acetate--CoA ligase.
Gene Ontology
Molecular Function
GO:0003987 acetate-CoA ligase activity
GO:0005524 ATP binding
GO:0016208 AMP binding
GO:0016874 ligase activity
GO:0016877 ligase activity, forming carbon-sulfur bonds
GO:0046872 metal ion binding
Biological Process
GO:0006085 acetyl-CoA biosynthetic process
GO:0006935 chemotaxis
GO:0019427 acetyl-CoA biosynthetic process from acetate
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5jrh, PDBe:5jrh, PDBj:5jrh
PDBsum5jrh
PubMed27974467
UniProtQ8ZKF6|ACSA_SALTY Acetyl-coenzyme A synthetase (Gene Name=acs)

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