Structure of PDB 6y9d Chain I Binding Site BS01

Receptor Information

>6y9d Chain I (length=352) Species: 470 (Acinetobacter baumannii)

VEKLPEDFCANPDVAWTFPKVFYTSSQVFEHEKEAIFAKSWICVAHGSEL
AQPNDYITRKVIGENIVIIRGKDSVLRAFYNVCPHRGHELLSGSGKAKNV
ITCPYHAWTFKLDGSLALARNCDHVESFDKENSSMVPLKVEEYAGFVFIN
MDENATCVEDQLPGFAERLNQACGVIKDLKLAARFVTETPANWKVIVDNY
MECYHCGPAHPGFADSVQVDKYWHTTHQNWTLQYGFPEFHGFWTWPCTMF
NVPPGSNFMTVIYEFPVDAETTLQHYDIYFTNEELTQDQKDLIEWYRNVF
RPEDLNLVESVQRGLKSRGYRGQGRIMTDKQRSGISEHGIAYFQHLVAQY
HQ

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 6y9d Chain I Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6y9d Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
• Resolution: 1.97 Å
• Binding residue (original residue number in PDB): H208 H213 D323
• Binding residue (residue number reindexed from 1): H205 H210 D304
• Annotation score: 1

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

External links

• PDB: RCSB:6y9d, PDBe:6y9d, PDBj:6y9d
• PDBsum: 6y9d
• PubMed: 33158989
• UniProt: A0A059ZPP5