3LA4
Crystal structure of the first plant urease from Jack bean (Canavalia ensiformis)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009039 | molecular_function | urease activity |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0035550 | cellular_component | urease complex |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0043419 | biological_process | urea catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 841 |
| Chain | Residue |
| A | HIS407 |
| A | HIS409 |
| A | KCX490 |
| A | ASP633 |
| A | NI842 |
| A | PO4843 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NI A 842 |
| Chain | Residue |
| A | HIS545 |
| A | GLY550 |
| A | NI841 |
| A | PO4843 |
| A | KCX490 |
| A | HIS492 |
| A | HIS519 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 A 843 |
| Chain | Residue |
| A | HIS407 |
| A | HIS409 |
| A | ALA440 |
| A | KCX490 |
| A | HIS492 |
| A | HIS519 |
| A | HIS545 |
| A | GLY550 |
| A | ASP633 |
| A | ALA636 |
| A | NI841 |
| A | NI842 |
| A | PO4844 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 844 |
| Chain | Residue |
| A | HIS492 |
| A | GLU493 |
| A | ASP494 |
| A | HIS519 |
| A | HIS593 |
| A | ARG609 |
| A | PO4843 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACN A 845 |
| Chain | Residue |
| A | ARG222 |
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","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20471401","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LA4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GY7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H9M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"20471401","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LA4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GY7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H9M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"20471401","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
