Structure of PDB 1qal Chain A

Receptor sequence
>1qalA (length=718) Species: 562 (Escherichia coli) [Search protein sequence]
MVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLA
LQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQ
AVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIM
LDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFA
AAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNY
WAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPM
QIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKV
MYEGSLGGMIVPYGDPDIGWYFKAYLNSGDYGMGTLTSPIARGKDAPSNA
VLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELV
VRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAK
DDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAG
GPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQII
PYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPN
RSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHT
LLKPWNFFDETPTLGALK
3D structure
PDB1qal The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y369 N383 Y466 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y363 N377 Y460 H518 H520 H683
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
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 CU A H524 H526 H689 H518 H520 H683
BS02 CA A D533 L534 D535 D678 A679 D527 L528 D529 D672 A673
BS03 CA A E573 Y667 D670 E672 E567 Y661 D664 E666
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0006559 L-phenylalanine catabolic process
GO:0009308 amine metabolic process
GO:0019607 phenylethylamine catabolic process
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qal, PDBe:1qal, PDBj:1qal
PDBsum1qal
PubMed10387067
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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