Structure of PDB 2fty Chain C

Receptor sequence
>2ftyC (length=531) Species: 4934 (Lachancea kluyveri) [Search protein sequence]
PIYDLIIKNGIICTASDIYAAEIAVNNGKVQLIAASIDPSLGSEVIDAEG
AFITPGGIDAHVHVDEPLKLLGDVVDTMEHATRSAVAGGTTTVVAFSTQD
VSKKGPSALAESVKLDVDEYSEQTLYCDYGLHLILFQIEKPSVEARELLD
VQLQAAYNDYGVSSVKMFMTYPGLQISDYDIMSAMYATRKNGFTTMLHAE
NGDMVKWMIEALEEQGLTDAYYHGVSRPSIVEGEATNRAITLATTMDTPI
LFVHVSSPQAAEVIKQAQTKGLKVYAETCPQYALLSDAITRCGVGIDLSS
ISESPFTNPDDRFIGSKYICSPPIRPEGTQKSIWKGMNNGTFTIVGSDHC
SYNYYEKTSTASKHRAFDPENNKNGEFRYIPNGLPGVCTRMPLLYDYGYL
RGNLTSMMKLVEIQCTNPAKVYGMYPQKGSILPGVSDADLVIWYPDDSKK
EYNSKPKLITNKLMEHNCDYTPFEGIEIKNWPRYTIVKGKIVYKEGEILK
ENADGKYLKRGKSFMCTPKNEWVTEWRPKYE
3D structure
PDB2fty The Crystal Structures of Dihydropyrimidinases Reaffirm the Close Relationship between Cyclic Amidohydrolases and Explain Their Substrate Specificity.
ChainC
Resolution2.4 Å
3D
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
Enzyme Commision number 3.5.2.2: dihydropyrimidinase.
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 ZN C H62 H64 K167 H61 H63 K166
BS02 ZN C K167 H199 H255 K166 H198 H254
Gene Ontology
Molecular Function
GO:0004157 dihydropyrimidinase activity
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:2fty, PDBe:2fty, PDBj:2fty
PDBsum2fty
PubMed16517602
UniProtQ9P903|DPYS_LACK1 Dihydropyrimidinase (Gene Name=PYD2)

[Back to BioLiP]