Structure of PDB 8hfd Chain B

Receptor sequence
>8hfdB (length=447) Species: 562 (Escherichia coli) [Search protein sequence]
SFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVV
SPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVD
RASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVAG
IDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRV
TAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRAR
QEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFN
GEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMS
LPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEY
RHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ
3D structure
PDB8hfd Crystal Structure of Allantoinase from Escherichia coli BL21: A Molecular Insight into a Role of the Active Site Loops in Catalysis.
ChainB
Resolution2.07 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.2.5: allantoinase.
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 H59 H61 K146 D315 H58 H60 K145 D309
BS02 ZN B K146 H186 H242 K145 H180 H236
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:0006144 purine nucleobase metabolic process
GO:0006145 purine nucleobase catabolic process
GO:0009442 allantoin assimilation pathway
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8hfd, PDBe:8hfd, PDBj:8hfd
PDBsum8hfd
PubMed36677881
UniProtP77671|ALLB_ECOLI Allantoinase (Gene Name=allB)

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