Structure of PDB 6y9d Chain H

Receptor sequence
>6y9dH (length=352) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
VEKLPEDFCANPDVAWTFPKVFYTSSQVFEHEKEAIFAKSWICVAHGSEL
AQPNDYITRKVIGENIVIIRGKDSVLRAFYNVCPHRGHELLSGSGKAKNV
ITCPYHAWTFKLDGSLALARNCDHVESFDKENSSMVPLKVEEYAGFVFIN
MDENATCVEDQLPGFAERLNQACGVIKDLKLAARFVTETPANWKVIVDNY
MECYHCGPAHPGFADSVQVDKYWHTTHQNWTLQYGFPEFHGFWTWPCTMF
NVPPGSNFMTVIYEFPVDAETTLQHYDIYFTNEELTQDQKDLIEWYRNVF
RPEDLNLVESVQRGLKSRGYRGQGRIMTDKQRSGISEHGIAYFQHLVAQY
HQ
3D structure
PDB6y9d Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
ChainH
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 FE H H208 H213 D323 H205 H210 D304
BS02 FES H C86 H88 C106 Y108 H109 W111 C83 H85 C103 Y105 H106 W108
BS03 152 H Y203 C206 Y225 Q236 N270 Y295 F319 Y200 C203 Y222 Q233 N251 Y276 F300
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

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

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