1PJ8
Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1pj8a_ | Alpha and beta proteins (a/b) | Subtilisin-like | Subtilisin-like | Subtilases | Proteinase K | (Parengyodontium album ) [TaxId: 37998 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | Subtilisin-like | 8043920 | 3000226 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.40.50.200 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Peptidase S8/S53 domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00082 | Subtilase family (Peptidase_S8) | Subtilase family | Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7 ... | Domain | |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
---|---|---|---|---|
Proteinase K | ||||
B [auth I] | 6-residue peptide (N-Ac-PAPFPA-NH2) | - | - | - |
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR023828 | Peptidase S8, subtilisin, Ser-active site | Active Site | |
IPR010259 | Peptidase S8 propeptide/proteinase inhibitor I9 | Domain | |
IPR022398 | Peptidase S8, subtilisin, His-active site | Active Site | |
IPR000209 | Peptidase S8/S53 domain | Domain | |
IPR015500 | Peptidase S8, subtilisin-related | Family | |
IPR036852 | Peptidase S8/S53 domain superfamily | Homologous Superfamily | |
IPR023827 | Peptidase S8, subtilisin, Asp-active site | Active Site | |
IPR034193 | Proteinase K-like catalytic domain | Domain | |
IPR037045 | Peptidase S8 propeptide/proteinase inhibitor I9 superfamily | Homologous Superfamily |
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
B [auth I] | NH2 | AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 :  L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109 | :