Structure of PDB 6zgp Chain K

Receptor sequence
>6zgpK (length=359) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
AVEKLPEDFCANPDVAWTFPKVFYTSSQVFEHEKEAIFAKSWICVAHGSE
LAQPNDYITRKVIGENIVIIRGKDSVLRAFYNVCPHRGHELLSGSGKAKN
VITCPYHAWTFKLDGSLALARNCDHVESFDKENSSMVPLKVEEYAGFVFI
NMDENATCVEDQLPGFAERLNQACGVIKDLKLAARFVTETPANWKVIVDN
YMECYHCGPAHPGFADSVQVDKYWHTTHQNWTLQYGFARSSTDPEFHGFW
TWPCTMFNVPPGSNFMTVIYEFPVDAETTLQHYDIYFTNEELTQDQKDLI
EWYRNVFRPEDLNLVESVQRGLKSRGYRGQGRIMTDKQRSGISEHGIAYF
QHLVAQYHQ
3D structure
PDB6zgp Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
ChainK
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 K H208 H213 D323 H206 H211 D311
BS02 FES K C86 H88 R89 C106 Y108 H109 W111 C84 H86 R87 C104 Y106 H107 W109
BS03 QKQ K Y203 E205 Y225 Q236 F258 H259 G260 N270 P272 T279 Y295 Y315 F319 D323 Y201 E203 Y223 Q234 F246 H247 G248 N258 P260 T267 Y283 Y303 F307 D311 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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