Structure of PDB 1ejs Chain C

Receptor sequence

>1ejsC (length=566)

SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLKINEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDL
GAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVK
RYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGG
MIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGV
AERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELIT
SEPADVLPMAQRYFLF

3D structure

• PDB: 1ejs Kinetic and structural characterization of urease active site variants.
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H1134 H1136 K1217 N1219 D1221 H1246 H1272 H1320 R1336 D1360
• Catalytic site (residue number reindexed from 1): H133 H135 K216 N218 D220 H245 H271 H319 R335 D359
• 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 D359

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

External links

• PDB: RCSB:1ejs, PDBe:1ejs, PDBj:1ejs
• PDBsum: 1ejs
• PubMed: 10913264
• UniProt: P18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)