Structure of PDB 6zgp Chain J

Receptor sequence
>6zgpJ (length=356) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
AVEKLPEDFCANPDVAWTFPKVFYTSSQVFEHEKEAIFAKSWICVAHGSE
LAQPNDYITRKVIGENIVIIRGKDSVLRAFYNVCPHRGHELLSGSGKAKN
VITCPYHAWTFKLDGSLALARNCDHVESFDKENSSMVPLKVEEYAGFVFI
NMDENATCVEDQLPGFAERLNQACGVIKDLKLAARFVTETPANWKVIVDN
YMECYHCGPAHPGFADSVQVDKYWHTTHQNWTLQYGFATDPEFHGFWTWP
CTMFNVPPGSNFMTVIYEFPVDAETTLQHYDIYFTNEELTQDQKDLIEWY
RNVFRPEDLNLVESVQRGLKSRGYRGQGRIMTDKQRSGISEHGIAYFQHL
VAQYHQ
3D structure
PDB6zgp Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
ChainJ
Resolution2.01 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) H107 E203 H206 H211
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 J H208 H213 D323 H206 H211 D308
BS02 FES J C86 H88 H91 C106 Y108 H109 W111 C84 H86 H89 C104 Y106 H107 W109
BS03 QKQ J Y203 E205 C206 F216 Y225 Q236 F258 H259 G260 N270 T279 Y295 Y315 F319 D323 Y201 E203 C204 F214 Y223 Q234 F243 H244 G245 N255 T264 Y280 Y300 F304 D308 MOAD: Ki=1.09uM
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:6zgp, PDBe:6zgp, PDBj:6zgp
PDBsum6zgp
PubMed33158989
UniProtA0A059ZPP5

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