Structure of PDB 1eju Chain C

Receptor sequence
>1ejuC (length=553) [Search protein sequence]
SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLMAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAM
GRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALT
HGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINAS
IPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVV
KGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRY
FLF
3D structure
PDB1eju Kinetic and structural characterization of urease active site variants.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H1134 H1136 K1217 H1219 D1221 H1246 H1272 R1336 D1360
Catalytic site (residue number reindexed from 1) H133 H135 K216 H218 D220 H245 H271 R322 D346
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 K1217 H1246 H1272 K216 H245 H271
BS02 NI C H1134 H1136 K1217 D1360 H133 H135 K216 D346
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:1eju, PDBe:1eju, PDBj:1eju
PDBsum1eju
PubMed10913264
UniProtP18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)

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