1KRA
CRYSTAL STRUCTURE OF KLEBSIELLA AEROGENES UREASE, ITS APOENZYME AND TWO ACTIVE SITE MUTANTS
Replaces: 3KAUFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
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 | 0005515 | molecular_function | protein binding |
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 | ACT |
Number of Residues | 2 |
Details | RESIDUE IMPLICATED IN CATALYSIS |
Chain | Residue |
C | HIS219 |
C | HIS320 |
site_id | NIL |
Number of Residues | 7 |
Details | EMPTY NICKEL METALLOCENTER |
Chain | Residue |
C | HIS134 |
C | HIS136 |
C | LYS217 |
C | HIS246 |
C | HIS272 |
C | ASP360 |
C | GLY173 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
C | HIS320 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
C | HIS134 | |
C | HIS136 | |
C | HIS219 | |
C | HIS246 | |
C | HIS272 | |
C | ASP360 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: via carbamate group |
Chain | Residue | Details |
C | LYS217 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_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 |
Chain | Residue | Details |
C | LYS217 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 8318888, 7754395, 8683579, 8702515, 8718850, 9201965, 9558361, Barrios2000 |
Chain | Residue | Details |
C | ASP221 | |
C | HIS320 | |
C | ARG336 | |
C | HIS219 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 87 |
Chain | Residue | Details |
C | HIS134 | metal ligand |
C | ASP360 | activator, metal ligand |
C | HIS136 | metal ligand |
C | LYS217 | activator, metal ligand |
C | HIS219 | proton acceptor, proton donor, proton relay |
C | ASP221 | activator, proton acceptor, proton donor |
C | HIS246 | metal ligand |
C | HIS272 | metal ligand |
C | HIS320 | proton acceptor, proton donor |
C | ARG336 | activator |