Structure of PDB 1gkr Chain D

Receptor sequence
>1gkrD (length=451) Species: 43663 (Paenarthrobacter aurescens) [Search protein sequence]
MFDVIVKNCRLVSSDGITEADILVKDGKVAAISADTSDVEASRTIDAGGK
FVMPGVVDEHVHIIDMDLKNRYGRFELDSESAAVGGITTIIEMPITFPPT
TTLDAFLEKKKQAGQRLKVDFALYGGGVPGNLPEIRKMHDAGAVGFKSMM
AASVPGMFDAVSDGELFEIFQEIAACGSVIVVHAENETIIQALQKQIKAA
GGKDMAAYEASQPVFQENEAIQRALLLQKEAGCRLIVLHVSNPDGVELIH
QAQSEGQDVHCESGPQYLNITTDDAERIGPYMKVAPPVRSAEMNIRLWEQ
LENGLIDTLGSDHGGHPVEDKEPGWKDVWKAGNGALGLETSLPMMLTNGV
NKGRLSLERLVEVMCEKPAKLFGIYPQKGTLQVGSDADLLILDLDIDTKV
DASQFRSLHKYSPFDGMPVTGAPVLTMVRGTVVAEKGEVLVEQGFGQFVT
R
3D structure
PDB1gkr The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity.
ChainD
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.2.-
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 K147 H183 H239 K147 H183 H239
BS02 ZN D H60 H62 K147 D312 H60 H62 K147 D312
Gene Ontology
Molecular Function
GO:0004038 allantoinase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
GO:0050897 cobalt ion binding
Biological Process
GO:0000256 allantoin catabolic process
GO:0006145 purine nucleobase catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:1gkr, PDBe:1gkr, PDBj:1gkr
PDBsum1gkr
PubMed12093275
UniProtP81006|HYDL_PAEAU L-hydantoinase (Gene Name=lhyD)

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