Structure of PDB 2ubp Chain C

Receptor sequence

>2ubpC (length=570) Species: 1474 (Sporosarcina pasteurii)

MKINRQQYAESYGPTVGDEVRLADTDLWIEVEKDYTTYGDEVNFGGGKVL
REGMGENGTYTRTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKG
GNPDIMDGVTPNMIVGTATEVIAAEGKIVTAGGIDTHVHFINPDQVDVAL
ANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKG
HGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHS
DTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSS
TNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDI
LHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDN
FRLKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRV
IKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSI
QQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDG
EVLTCEPVKELPMAQRYFLF

3D structure

• PDB: 2ubp A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
• Chain: C
• Resolution: 2.0 Å

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	NI	C	K220 H249 H275	K220 H249 H275
BS02	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

External links

• PDB: RCSB:2ubp, PDBe:2ubp, PDBj:2ubp
• PDBsum: 2ubp
• PubMed: 10368287
• UniProt: P41020|URE1_SPOPA Urease subunit alpha (Gene Name=ureC)