Structure of PDB 8q2e Chain C

Receptor sequence
>8q2eC (length=570) Species: 1474 (Sporosarcina pasteurii) [Search protein sequence]
MKINRQQYAESYGPTVGDQVRLADTDLWIEVEKDYTTYGDEANFGGGKVL
REGMGENGTYTRTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKG
GNPDIMDGVTPNMIVGTATEVIAAEGKIVTAGGIDTHVHFINPDQVDVAL
ANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKG
HGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHS
DTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSS
TNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDI
LHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDN
FRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRV
IKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSI
QQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDG
EVLTCEPVKELPMAQRYFLF
3D structure
PDB8q2e Kinetic and structural details of urease inactivation by thiuram disulphides.
ChainC
Resolution1.68 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.5: urease.
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 IS9 C V321 C322 V321 C322
BS02 NI C K220 H249 H275 K220 H249 H275
BS03 NI C H137 H139 K220 D363 H137 H139 K220 D363
Gene Ontology
Molecular Function
GO:0009039 urease activity
GO:0016151 nickel cation binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0043419 urea catabolic process
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:8q2e, PDBe:8q2e, PDBj:8q2e
PDBsum8q2e
PubMed37879152
UniProtP41020|URE1_SPOPA Urease subunit alpha (Gene Name=ureC)

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