Structure of PDB 2o7e Chain E

Receptor sequence
>2o7eE (length=514) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence]
KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEARLGAVIREAR
HVYGLTTGFGPLANRLISGENVRTLQANLVHFLASGVGPVLDWTTARAMV
LARLVSIAQGASGASEGTIARLIDLLNSELAPAVPSRGTVGGDLTPLAHM
VLCLQGRGDFLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALSDLRPHPGQKD
AAARLRARVDGSARVVRHVIAERRLDAGDIGTEPEAGQDAYSLRCAPQVL
GAGFDTLAWHDRVLTIELNAVTDNPVFPPDGSVPALHGGNFMGQHVALTS
DALATAVTVLAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLCREKIDRWAEI
LAILALCLAQAAELRCGSGLDGVSPAGKKLVQALREQFPPLETDRPLGQE
IAALATHLLQQSPV
3D structure
PDB2o7e Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
ChainE
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y60 G67 L90 N203 Y300 R303 F350 Q436
Catalytic site (residue number reindexed from 1) Y53 G60 L83 N194 Y291 R294 F341 Q427
Enzyme Commision number 4.3.1.23: tyrosine ammonia-lyase.
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 PMI E Y60 X149 L153 N203 N333 F350 Y53 X142 L144 N194 N324 F341
BS02 PMI E Y300 R303 Y291 R294
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016841 ammonia-lyase activity
GO:0042802 identical protein binding
GO:0052883 tyrosine ammonia-lyase activity
Biological Process
GO:0006572 tyrosine catabolic process
GO:0009698 phenylpropanoid metabolic process
GO:0009699 phenylpropanoid biosynthetic process
GO:0044550 secondary metabolite biosynthetic process
GO:0051289 protein homotetramerization

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Molecular Function

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Biological Process
External links
PDB RCSB:2o7e, PDBe:2o7e, PDBj:2o7e
PDBsum2o7e
PubMed17185228
UniProtQ3IWB0|TALY_CERS4 Tyrosine ammonia-lyase (Gene Name=hutH)

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