Structure of PDB 2fvk Chain B

Receptor sequence
>2fvkB (length=532) Species: 4934 (Lachancea kluyveri) [Search protein sequence]
PIYDLIIKNGIICTASDIYAAEIAVNNGKVQLIAASIDPSLGSEVIDAEG
AFITPGGIDAHVHVDEPLKLLGDVVDTMEHATRSAVAGGTTTVVAFSTQD
VSKKGPSALAESVKLDVDEYSEQTLYCDYGLHLILFQIEKPSVEARELLD
VQLQAAYNDYGVSSVKMFMTYPGLQISDYDIMSAMYATRKNGFTTMLHAE
NGDMVKWMIEALEEQGLTDAYYHGVSRPSIVEGEATNRAITLATTMDTPI
LFVHVSSPQAAEVIKQAQTKGLKVYAETCPQYALLSDAITRCHGVGIDLS
SISESPFTNPDDRFIGSKYICSPPIRPEGTQKSIWKGMNNGTFTIVGSDH
CSYNYYEKTSTASKHRAFDPENNKNGEFRYIPNGLPGVCTRMPLLYDYGY
LRGNLTSMMKLVEIQCTNPAKVYGMYPQKGSILPGVSDADLVIWYPDDSK
KEYNSKPKLITNKLMEHNCDYTPFEGIEIKNWPRYTIVKGKIVYKEGEIL
KENADGKYLKRGKSFMCTPKNEWVTEWRPKYE
3D structure
PDB2fvk The Crystal Structures of Dihydropyrimidinases Reaffirm the Close Relationship between Cyclic Amidohydrolases and Explain Their Substrate Specificity.
ChainB
Resolution2.4 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 B H62 H64 D358 H61 H63 D349
BS02 ZN B H199 H255 H198 H254
BS03 DUC B H255 C330 S331 D358 N392 H254 C321 S322 D349 N383
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:2fvk, PDBe:2fvk, PDBj:2fvk
PDBsum2fvk
PubMed16517602
UniProtQ9P903|DPYS_LACK1 Dihydropyrimidinase (Gene Name=PYD2)

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