Structure of PDB 1qaf Chain B

Receptor sequence
>1qafB (length=721) Species: 562 (Escherichia coli) [Search protein sequence]
HMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPL
ALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIK
QAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVI
MLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEF
AAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGN
YWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKP
MQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRK
VMYEGSLGGMIVPYGDPDIGWYFKAYLESGDYGMGTLTSPIARGKDAPSN
AVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERREL
VVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETA
KDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTA
GGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQI
IPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYP
NRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVH
TLLKPWNFFDETPTLGALKKD
3D structure
PDB1qaf The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y369 E383 Y466 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y364 E378 Y461 H519 H521 H684
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 B H524 H526 H689 H519 H521 H684
BS02 CA B D533 L534 D535 D678 A679 D528 L529 D530 D673 A674
BS03 CA B E573 Y667 E672 E568 Y662 E667
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1qaf, PDBe:1qaf, PDBj:1qaf
PDBsum1qaf
PubMed10387067
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

[Back to BioLiP]