1KRA

CRYSTAL STRUCTURE OF KLEBSIELLA AEROGENES UREASE, ITS APOENZYME AND TWO ACTIVE SITE MUTANTS

Replaces:  3KAU

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0009039	molecular_function	urease activity
A	0016151	molecular_function	nickel cation binding
A	0016787	molecular_function	hydrolase activity
A	0019627	biological_process	urea metabolic process
A	0043419	biological_process	urea catabolic process
B	0005737	cellular_component	cytoplasm
B	0009039	molecular_function	urease activity
B	0016787	molecular_function	hydrolase activity
B	0035550	cellular_component	urease complex
B	0043419	biological_process	urea catabolic process
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0009039	molecular_function	urease activity
C	0016151	molecular_function	nickel cation binding
C	0016787	molecular_function	hydrolase activity
C	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C	0043419	biological_process	urea catabolic process
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	ACT
Number of Residues	2
Details	RESIDUE IMPLICATED IN CATALYSIS

Chain	Residue
C	HIS219
C	HIS320

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site_id	NIL
Number of Residues	7
Details	EMPTY NICKEL METALLOCENTER

Chain	Residue
C	HIS134
C	HIS136
C	LYS217
C	HIS246
C	HIS272
C	ASP360
C	GLY173

---

Functional Information from PROSITE/UniProt

site_id	PS00145
Number of Residues	17
Details	UREASE_2 Urease active site. MVCHHLdpdIaeDVaFA

Chain	Residue	Details
C	MET317-ALA333

---

site_id	PS01120
Number of Residues	14
Details	UREASE_1 Urease nickel ligands signature. TAGGIDtHIHwicP

Chain	Residue	Details
C	THR127-PRO140

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	438
Details	Domain: {"description":"Urease","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"description":"via carbamate group"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10913264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7754395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8718850","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8318888, 7754395, 8683579, 8702515, 8718850, 9201965, 9558361, Barrios2000

Chain	Residue	Details
C	ASP221
C	HIS320
C	ARG336
C	HIS219

---

site_id	MCSA1
Number of Residues	10
Details	M-CSA 87

Chain	Residue	Details
C	HIS134	metal ligand
C	ASP360	activator, metal ligand
C	HIS136	metal ligand
C	LYS217	activator, metal ligand
C	HIS219	proton acceptor, proton donor, proton relay
C	ASP221	activator, proton acceptor, proton donor
C	HIS246	metal ligand
C	HIS272	metal ligand
C	HIS320	proton acceptor, proton donor
C	ARG336	activator

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