Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6G48

Sporosarcina pasteurii urease inhibited by silver

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	AC1
Number of Residues	6
Details	binding site for residue EDO A 201

Chain	Residue
A	ASN4
A	LYS10
A	HOH303
A	HOH326
C	PHE568
C	PHE570

site_id	AC2
Number of Residues	9
Details	binding site for residue EDO A 202

Chain	Residue
A	PHE86
A	PRO87
A	ASP88
C	VAL309
C	ASN310
C	LYS559
A	GLY50
A	LYS51
A	THR52

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 203

Chain	Residue
A	CXM1
A	ASP79
A	GLN81
A	HOH301
C	THR470
C	GLN472

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 204

Chain	Residue
A	MET70
A	GLU71
C	ARG566

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO B 201

Chain	Residue
B	GLN41
B	HOH305
B	HOH317
B	HOH323
B	HOH338
C	HIS323
C	LEU325

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 B 202

Chain	Residue
B	THR29
B	ILE30
B	ARG31
B	HOH307

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 203

Chain	Residue
B	LEU112
B	ARG116
B	HOH302

site_id	AC8
Number of Residues	8
Details	binding site for residue NI C 601

Chain	Residue
C	KCX220
C	HIS222
C	HIS249
C	HIS275
C	GLY280
C	NI602
C	OH603
C	HOH701

site_id	AC9
Number of Residues	7
Details	binding site for residue NI C 602

Chain	Residue
C	HIS137
C	HIS139
C	KCX220
C	ASP363
C	NI601
C	OH603
C	HOH704

site_id	AD1
Number of Residues	9
Details	binding site for residue OH C 603

Chain	Residue
C	HIS137
C	KCX220
C	HIS275
C	ASP363
C	NI601
C	NI602
C	HOH701
C	HOH703
C	HOH704

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO C 604

Chain	Residue
C	GLY45
C	GLY46
C	ASP224
C	HIS323
C	SO4612
C	HOH801

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO C 605

Chain	Residue
B	ASP101
C	PRO229
C	HOH809

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO C 606

Chain	Residue
C	ASP286
C	ALA289
C	ILE537
C	ILE539
C	HOH765

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO C 607

Chain	Residue
B	SER71
C	TYR12
C	LYS48

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO C 608

Chain	Residue
C	ASP34
C	THR36
C	TYR38
C	HOH855
C	HOH909

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO C 609

Chain	Residue
C	HIS422
C	GLU423
C	GLY430
C	GLN501
C	HOH737

site_id	AD8
Number of Residues	5
Details	binding site for residue SO4 C 610

Chain	Residue
C	GLU64
C	SER204
C	ILE205
C	HOH793
C	HOH838

site_id	AD9
Number of Residues	4
Details	binding site for residue SO4 C 611

Chain	Residue
C	VAL558
C	LYS559
C	GLU560
C	HOH922

site_id	AE1
Number of Residues	12
Details	binding site for residue SO4 C 612

Chain	Residue
C	GLU223
C	HIS249
C	GLY280
C	HIS323
C	ARG339
C	MET367
C	EDO604
C	AG613
C	AG614
C	HOH701
C	HOH759
C	HIS222

site_id	AE2
Number of Residues	4
Details	binding site for residue AG C 613

Chain	Residue
C	CYS322
C	HIS323
C	SO4612
C	AG614

site_id	AE3
Number of Residues	5
Details	binding site for residue AG C 614

Chain	Residue
C	CYS322
C	MET367
C	SO4612
C	AG613
C	HOH966

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	MET320-ALA336

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

Chain	Residue	Details
C	THR130-PRO143

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}}]}

Chain

Residue

Details

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":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}},{"source":"PDB","id":"1IE7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UBP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2UBP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UBP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)