Structure of PDB 4ubp Chain C

Receptor sequence
>4ubpC (length=570) Species: 1474 (Sporosarcina pasteurii) [Search protein sequence]
MKINRQQYAESYGPTVGDEVRLADTDLWIEVEKDYTTYGDEVNFGGGKVL
REGMGENGTYTRTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKG
GNPDIMDGVTPNMIVGTATEVIAAEGKIVTAGGIDTHVHFINPDQVDVAL
ANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKG
HGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHS
DTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSS
TNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDI
LHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDN
FRLKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRV
IKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSI
QQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDG
EVLTCEPVKELPMAQRYFLF
3D structure
PDB4ubp The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution.
ChainC
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H137 H139 K220 H222 D224 H249 H275 H323 R339 D363
Catalytic site (residue number reindexed from 1) H137 H139 K220 H222 D224 H249 H275 H323 R339 D363
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 HAE C H137 A170 K220 H222 H249 H275 D363 H137 A170 K220 H222 H249 H275 D363 MOAD: Ki=2.6uM
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:4ubp, PDBe:4ubp, PDBj:4ubp
PDBsum4ubp
PubMed10766443
UniProtP41020|URE1_SPOPA Urease subunit alpha (Gene Name=ureC)

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