1EJS
Crystal Structure of the H219N Variant of Klebsiella Aerogenes Urease
Functional 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 | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NI C 4774 |
Chain | Residue |
C | HOH500 |
C | HOH501 |
C | KCX1217 |
C | HIS1246 |
C | HIS1272 |
C | GLY1277 |
C | NI4775 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NI C 4775 |
Chain | Residue |
C | HIS1134 |
C | HIS1136 |
C | KCX1217 |
C | ASP1360 |
C | NI4774 |
C | HOH500 |
C | HOH502 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"description":"via carbamate group"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10913264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7754395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8718850","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1kra |
Chain | Residue | Details |
C | ASN1219 | |
C | ARG1336 | |
C | HIS1320 | |
C | ASP1221 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 87 |
Chain | Residue | Details |