Structure of PDB 2fvm Chain D

Receptor sequence
>2fvmD (length=532) Species: 4934 (Lachancea kluyveri) [Search protein sequence]
PIYDLIIKNGIICTASDIYAAEIAVNNGKVQLIAASIDPSLGSEVIDAEG
AFITPGGIDAHVHVDEPLKLLGDVVDTMEHATRSAVAGGTTTVVAFSTQD
VSKKGPSALAESVKLDVDEYSEQTLYCDYGLHLILFQIEKPSVEARELLD
VQLQAAYNDYGVSSVKMFMTYPGLQISDYDIMSAMYATRKNGFTTMLHAE
NGDMVKWMIEALEEQGLTDAYYHGVSRPSIVEGEATNRAITLATTMDTPI
LFVHVSSPQAAEVIKQAQTKGLKVYAETCPQYALLSDAITRCHVGIDLSS
ISESPFTNPDDRFIGSKYICSPPIRPEGTQKSIWKGMNNGTFTIVGSDHC
SYNYYEKTSTASKHRAFDPENNKNGEFRYIPNGLPGVCTRMPLLYDYGYL
RGNLTSMMKLVEIQCTNPAKVYGMYPQKGSILPGVSDADLVIWYPDDSKK
EYNSKPKLITNKLMEHNCDYTPFEGIEIKNWPRYTIVKGKIVYKEGEILK
ENADGKYLKRGKSFMCTPKNEWVTEWRPKYES
3D structure
PDB2fvm The Crystal Structures of Dihydropyrimidinases Reaffirm the Close Relationship between Cyclic Amidohydrolases and Explain Their Substrate Specificity.
ChainD
Resolution2.45 Å
3D
structure
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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 D H62 H64 K167 D358 H61 H63 K166 D348
BS02 ZN D 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

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Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:2fvm, PDBe:2fvm, PDBj:2fvm
PDBsum2fvm
PubMed16517602
UniProtQ9P903|DPYS_LACK1 Dihydropyrimidinase (Gene Name=PYD2)

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