Structure of PDB 6y9d Chain B Binding Site BS02

Receptor Information
>6y9d Chain B (length=352) Species: 470 (Acinetobacter baumannii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VEKLPEDFCANPDVAWTFPKVFYTSSQVFEHEKEAIFAKSWICVAHGSEL
AQPNDYITRKVIGENIVIIRGKDSVLRAFYNVCPHRGHELLSGSGKAKNV
ITCPYHAWTFKLDGSLALARNCDHVESFDKENSSMVPLKVEEYAGFVFIN
MDENATCVEDQLPGFAERLNQACGVIKDLKLAARFVTETPANWKVIVDNY
MECYHCGPAHPGFADSVQVDKYWHTTHQNWTLQYGFPEFHGFWTWPCTMF
NVPPGSNFMTVIYEFPVDAETTLQHYDIYFTNEELTQDQKDLIEWYRNVF
RPEDLNLVESVQRGLKSRGYRGQGRIMTDKQRSGISEHGIAYFQHLVAQY
HQ
Ligand information
Ligand IDFES
InChIInChI=1S/2Fe.2S
InChIKeyNIXDOXVAJZFRNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04[Fe]1S[Fe]S1
CACTVS 3.341
OpenEye OEToolkits 1.5.0		S1[Fe]S[Fe]1
FormulaFe2 S2
NameFE2/S2 (INORGANIC) CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain6y9d Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6y9d Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		C86 H88 R89 H91 C106 Y108 H109 W111
Binding residue
(residue number reindexed from 1)		C83 H85 R86 H88 C103 Y105 H106 W108
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H109 E205 H208 H213
Catalytic site (residue number reindexed from 1) H106 E202 H205 H210
Enzyme Commision number 1.14.13.239: carnitine monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009437 carnitine metabolic process
GO:0044237 cellular metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6y9d, PDBe:6y9d, PDBj:6y9d
PDBsum6y9d
PubMed33158989
UniProtA0A059ZPP5

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