5A6T
1.65 A resolution Sulphite inhibited Sporosarcina pasteurii urease
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 1571 |
Chain | Residue |
C | KCX220 |
C | HIS222 |
C | HIS249 |
C | HIS275 |
C | GLY280 |
C | NI1572 |
C | SO31573 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI C 1572 |
Chain | Residue |
C | KCX220 |
C | ASP363 |
C | NI1571 |
C | SO31573 |
C | HIS137 |
C | HIS139 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SO3 C 1573 |
Chain | Residue |
C | HIS137 |
C | HIS139 |
C | ALA170 |
C | KCX220 |
C | HIS222 |
C | HIS249 |
C | HIS275 |
C | GLY280 |
C | ASP363 |
C | ALA366 |
C | NI1571 |
C | NI1572 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 1574 |
Chain | Residue |
C | ASP34 |
C | THR36 |
C | TYR38 |
C | HOH2038 |
C | HOH2050 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 1101 |
Chain | Residue |
A | GLY50 |
A | LYS51 |
A | THR52 |
A | PHE86 |
A | ASP88 |
A | HOH2096 |
C | VAL309 |
C | ASN310 |
C | LYS559 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 1575 |
Chain | Residue |
C | ASP286 |
C | ALA289 |
C | ILE537 |
C | ILE539 |
C | HOH2224 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 1576 |
Chain | Residue |
C | TYR35 |
C | TYR83 |
C | ILE97 |
C | GLU429 |
C | HOH2035 |
C | HOH2399 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 1577 |
Chain | Residue |
B | ASP101 |
B | HOH2119 |
C | PRO229 |
C | ASP233 |
C | HOH2203 |
C | HOH2231 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1127 |
Chain | Residue |
B | HOH2070 |
C | GLY46 |
C | LEU325 |
C | HOH2193 |
C | HOH2264 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 1102 |
Chain | Residue |
A | ASN4 |
A | ALA6 |
A | LYS10 |
A | HOH2089 |
A | HOH2097 |
C | PHE568 |
C | PHE570 |
C | HOH2279 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1128 |
Chain | Residue |
B | ARG116 |
B | HOH2133 |
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:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10368287","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10766443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11713685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15038715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30969470","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"268","lastPage":"273","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-ray data at 1.65-A resolution.","authors":["Benini S.","Rypniewski W.R.","Wilson K.S.","Ciurli S.","Mangani S."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050231"}]}},{"source":"PDB","id":"1IE7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UBP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2UBP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UBP","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |