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1E9Y

Crystal structure of Helicobacter pylori urease in complex with acetohydroxamic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0009039molecular_functionurease activity
A0016151molecular_functionnickel cation binding
A0016787molecular_functionhydrolase activity
A0035550cellular_componenturease complex
A0043419biological_processurea catabolic process
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0009039molecular_functionurease activity
B0016151molecular_functionnickel cation binding
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0043419biological_processurea catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HAE B 800
ChainResidue
BALA169
BNI3002
BKCX219
BHIS221
BHIS248
BHIS274
BGLY279
BASP362
BALA365
BNI3001

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI B 3001
ChainResidue
BKCX219
BHIS248
BHIS274
BGLY279
BHAE800
BNI3002

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI B 3002
ChainResidue
BHIS136
BHIS138
BKCX219
BASP362
BHAE800
BNI3001

Functional Information from PROSITE/UniProt
site_idPS01120
Number of Residues14
DetailsUREASE_1 Urease nickel ligands signature. TAGGIDtHIHfisP
ChainResidueDetails
BTHR129-PRO142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues101
DetailsRegion: {"description":"Urease gamma"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues135
DetailsRegion: {"description":"Urease beta"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"via carbamate group"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11373617","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kra
ChainResidueDetails
BHIS221
BARG338
BASP223
BHIS322

244693

PDB entries from 2025-11-12

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