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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2UBP

STRUCTURE OF NATIVE UREASE FROM BACILLUS PASTEURII

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009039molecular_functionurease activity
A0016151molecular_functionnickel cation binding
A0016787molecular_functionhydrolase activity
A0019627biological_processurea metabolic process
A0043419biological_processurea catabolic process
B0005737cellular_componentcytoplasm
B0009039molecular_functionurease activity
B0016787molecular_functionhydrolase activity
B0035550cellular_componenturease complex
B0043419biological_processurea catabolic process
C0005737cellular_componentcytoplasm
C0009039molecular_functionurease activity
C0016151molecular_functionnickel cation binding
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0043419biological_processurea catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 C 900
ChainResidue
CHIS249
CGLY280
CHIS323
CARG339
CHOH972
CHOH1046
CHOH1167
CHOH1168
CHOH1245
CHIS222
CGLU223
CASP224
site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NI C 901
ChainResidue
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
CNI902
CHOH972
CHOH990
site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NI C 902
ChainResidue
CHIS137
CHIS139
CKCX220
CASP363
CNI901
CHOH990
CHOH1043
site_idCAT
Number of Residues6
DetailsTHE COORDINATION OF THE 2 NICKEL 2+ METALLOCENTER IS COMPLETED BY A CLUSTER OF WATERS
ChainResidue
CHIS137
CHIS139
CKCX220
CHIS249
CHIS275
CASP363
Functional Information from PROSITE/UniProt
site_idPS00145
Number of Residues17
DetailsUREASE_2 Urease active site. MVCHHLkqnIpeDVaFA
ChainResidueDetails
CMET320-ALA336
site_idPS01120
Number of Residues14
DetailsUREASE_1 Urease nickel ligands signature. TAGGIDtHVHfinP
ChainResidueDetails
CTHR130-PRO143
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsBinding 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"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding 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"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kra
ChainResidueDetails
CHIS323
CASP224
CARG339
CHIS222

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PDB entries from 2025-12-17

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