Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5FSD

1.75 A resolution 2,5-dihydroxybenzensulfonate inhibited Sporosarcina pasteurii urease

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	8
Details	BINDING SITE FOR RESIDUE NI C 600

Chain	Residue
C	KCX220
C	HIS222
C	HIS249
C	HIS275
C	GLY280
C	NI601
C	OH1584
C	HOH2165

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NI C 601

Chain	Residue
C	HIS139
C	KCX220
C	ASP363
C	NI600
C	OH1584
C	HOH2143
C	HIS137

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1572

Chain	Residue
C	ASP34
C	THR36
C	TYR38
C	HOH2040
C	HOH2054
C	HOH2406

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 1573

Chain	Residue
C	TYR60
C	ASN65
C	ILE114
C	SO41585
C	HOH2128

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 1574

Chain	Residue
C	HIS422
C	GLY430
C	GLN501
C	HOH2317

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1575

Chain	Residue
C	TYR93
C	GLU423
C	GLN501
C	ARG513
C	ILE514
C	HOH2409

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 1576

Chain	Residue
C	PRO143
C	GLY189
C	ARG478
C	HOH2410

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 1577

Chain	Residue
A	LYS10
A	THR85
A	THR90
C	PHE570
C	HOH2411

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1127

Chain	Residue
B	ASP101
B	HOH2118
C	PRO229
C	ASP233
C	HOH2204
C	HOH2234

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1578

Chain	Residue
B	HOH2069
C	GLY46
C	HIS323
C	LEU325
C	PHE335
C	HOH2194

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1579

Chain	Residue
B	SER71
B	THR73
C	ASN43
C	LYS48
C	HOH2010
C	HOH2015

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 1102

Chain	Residue
A	GLY50
A	LYS51
A	THR52
A	PHE86
A	ASP88
A	HOH2082
C	VAL309
C	ASN310
C	LYS559

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 1580

Chain	Residue
C	ASP286
C	ALA289
C	ILE539
C	HOH2225

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1103

Chain	Residue
A	TYR32
A	MET76
A	ASP78
A	ASP79

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1104

Chain	Residue
A	GLY27
A	LYS29
A	ASP67
A	ASP68
A	HOH2032
A	HOH2038

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1128

Chain	Residue
A	PHE42
A	GLU59
B	MET83
B	GLU84
B	HOH2098
B	HOH2143

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1581

Chain	Residue
C	TYR35
C	TYR83
C	ILE97
C	GLU429
C	HOH2037
C	HOH2048
C	HOH2412

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 1582

Chain	Residue
C	LYS33
C	TYR35
C	HOH2048

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 1583

Chain	Residue
C	HIS222
C	GLU223
C	HIS249
C	GLY280
C	HIS323
C	ARG339
C	HOH2196
C	HOH2199
C	HOH2243

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OH C 1584

Chain	Residue
C	HIS137
C	KCX220
C	HIS275
C	ASP363
C	NI600
C	NI601
C	HOH2143
C	HOH2165
C	HOH2243

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1585

Chain	Residue
C	SER204
C	ILE205
C	EDO1573
C	HOH2180
C	HOH2184

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1105

Chain	Residue
A	MET70
A	GLU71
C	ARG566

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 1129

Chain	Residue
B	ARG116
B	HOH2135

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1586

Chain	Residue
C	VAL558
C	LYS559
C	GLU560
C	HOH2397

site_id	CC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1130

Chain	Residue
B	THR29
B	ILE30
B	ARG31
B	HOH2052
B	HOH2053
B	HOH2081

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DBX C 1587

Chain	Residue
C	LYS169
C	VAL321
C	CYS322
C	PRO469
C	THR470
C	HOH2162
C	HOH2414

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DBX C 1588

Chain	Residue
C	GLN387
C	ARG388
C	THR554
C	CYS555
C	GLU556
C	HOH2415
C	HOH2416

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)