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1KRB

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
C0005515molecular_functionprotein binding
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 Residues6
DetailsBINDING SITE FOR RESIDUE NI C 574
ChainResidue
CKCX217
CHIS246
CHIS272
CGLY277
CNI575
CHOH577

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI C 575
ChainResidue
CHIS134
CHIS136
CKCX217
CASP360
CNI574
CHOH577

site_idACT
Number of Residues2
DetailsRESIDUE IMPLICATED IN CATALYSIS
ChainResidue
CALA219
CHIS320

site_idNIL
Number of Residues9
DetailsNICKEL METALLOCENTER
ChainResidue
CHIS134
CHIS136
CKCX217
CHIS246
CHIS272
CASP360
CNI574
CNI575
AMET1

Functional Information from PROSITE/UniProt
site_idPS00145
Number of Residues17
DetailsUREASE_2 Urease active site. MVCHHLdpdIaeDVaFA
ChainResidueDetails
CMET317-ALA333

site_idPS01120
Number of Residues14
DetailsUREASE_1 Urease nickel ligands signature. TAGGIDtHIHwicP
ChainResidueDetails
CTHR127-PRO140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
CHIS320

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
CHIS134
CHIS136
CALA219
CHIS246
CHIS272
CASP360

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: via carbamate group
ChainResidueDetails
CKCX217

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850
ChainResidueDetails
CKCX217

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kra
ChainResidueDetails
CASP221
CHIS320
CARG336
CALA219

site_idMCSA1
Number of Residues10
DetailsM-CSA 87
ChainResidueDetails
CHIS134metal ligand
CASP360activator, metal ligand
CHIS136metal ligand
CKCX217activator, metal ligand
CALA219proton acceptor, proton donor, proton relay
CASP221activator, proton acceptor, proton donor
CHIS246metal ligand
CHIS272metal ligand
CHIS320proton acceptor, proton donor
CARG336activator

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PDB entries from 2024-11-13

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