1X9Y
The prostaphopain B structure
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
| Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
|---|---|---|---|---|---|
| A | SCOP2 Family | Staphopain B prodomain | 8031350 | 4003676 | SCOP2 (2022-06-29) |
| A | SCOP2 Superfamily | Cystatin/monellin | 8043728 | 3000441 | SCOP2 (2022-06-29) |
| A | SCOP2B Superfamily | Cysteine proteinases | 8034081 | 3001808 | SCOP2B (2022-06-29) |
| B | SCOP2B Superfamily | Cysteine proteinases | 8034081 | 3001808 | SCOP2B (2022-06-29) |
| B | SCOP2B Superfamily | Cystatin/monellin | 8043728 | 3000441 | SCOP2B (2022-06-29) |
| C | SCOP2B Superfamily | Cystatin/monellin | 8043728 | 3000441 | SCOP2B (2022-06-29) |
| C | SCOP2B Superfamily | Cysteine proteinases | 8034081 | 3001808 | SCOP2B (2022-06-29) |
| D | SCOP2B Superfamily | Cystatin/monellin | 8043728 | 3000441 | SCOP2B (2022-06-29) |
| D | SCOP2B Superfamily | Cysteine proteinases | 8034081 | 3001808 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
| Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
|---|---|---|---|---|---|---|---|---|
| A | PF14731 | e1x9yA1 | A: a+b two layers | X: Cystatin-like | H: Cystatin/monellin (From Topology) | T: Cystatin/monellin | F: PF14731 | ECOD (1.6) |
| A | PF05543 | e1x9yA2 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: PF05543 | ECOD (1.6) |
| B | PF14731 | e1x9yB1 | A: a+b two layers | X: Cystatin-like | H: Cystatin/monellin (From Topology) | T: Cystatin/monellin | F: PF14731 | ECOD (1.6) |
| B | PF05543 | e1x9yB2 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: PF05543 | ECOD (1.6) |
| C | PF14731 | e1x9yC1 | A: a+b two layers | X: Cystatin-like | H: Cystatin/monellin (From Topology) | T: Cystatin/monellin | F: PF14731 | ECOD (1.6) |
| C | PF05543 | e1x9yC2 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: PF05543 | ECOD (1.6) |
| D | PF14731 | e1x9yD1 | A: a+b two layers | X: Cystatin-like | H: Cystatin/monellin (From Topology) | T: Cystatin/monellin | F: PF14731 | ECOD (1.6) |
| D | PF05543 | e1x9yD2 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: PF05543 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
| Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
|---|---|---|---|---|---|---|
| A | 3.10.500.10 | Alpha Beta | Roll | prostaphopain b, domain 1 | Staphopain proregion domain | CATH (4.3.0) |
| A | 3.90.70.10 | Alpha Beta | Alpha-Beta Complex | Cathepsin B | Chain A | CATH (4.3.0) |
| B | 3.10.500.10 | Alpha Beta | Roll | prostaphopain b, domain 1 | Staphopain proregion domain | CATH (4.3.0) |
| B | 3.90.70.10 | Alpha Beta | Alpha-Beta Complex | Cathepsin B | Chain A | CATH (4.3.0) |
| C | 3.10.500.10 | Alpha Beta | Roll | prostaphopain b, domain 1 | Staphopain proregion domain | CATH (4.3.0) |
| C | 3.90.70.10 | Alpha Beta | Alpha-Beta Complex | Cathepsin B | Chain A | CATH (4.3.0) |
| D | 3.10.500.10 | Alpha Beta | Roll | prostaphopain b, domain 1 | Staphopain proregion domain | CATH (4.3.0) |
| D | 3.90.70.10 | Alpha Beta | Alpha-Beta Complex | Cathepsin B | Chain A | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
| Chains | Accession | Name | Description | Comments | Source |
|---|---|---|---|---|---|
| PF14731 | Staphopain proregion (Staphopain_pro) | Staphopain proregion | This domain is the proregion of the cysteine protease staphopain. Like many papain type peptidases, staphopain is synthesised as an inactive precursor and cleavage of the proregion is required for activation. This proregion has a half-barrel or barre ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
| Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
|---|---|---|---|---|
| cysteine proteinase |
InterPro: Protein Family Classification InterPro Database Homepage
| Chains | Accession | Name | Type |
|---|---|---|---|
| IPR038765 | Papain-like cysteine peptidase superfamily | Homologous Superfamily | |
| IPR028076 | Staphopain proregion | Domain | |
| IPR025660 | Cysteine peptidase, histidine active site | Active Site | |
| IPR037155 | Staphopain proregion superfamily | Homologous Superfamily | |
| IPR008750 | Staphopain peptidase C47 | Family | |
| IPR046350 | Cystatin superfamily | Homologous Superfamily |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
| Chains | Enzyme Name | Description | Catalytic Residues |
|---|---|---|---|
| staphopain M-CSA #805 | Staphopain B is a possible virulence factor from Staphylococcus aureus, and is a member of the papain superfamily of cysteine proteases. It is able to degrade elastin, fibrogen, fibronectin and kininogen. Exhibits a strong preference for substrates where arginine is preceded by a hydrophobic amino acid. Promotes detachment of primary human keratinocytes. Along with other extracellular proteases is involved in colonization and infection of human tissues Staphostatin B is a specific inhibitor of staphopain B encoded in the same operon. Inhibition of staphopains is a target for treatment of antibiotic-resistant S. aureus infections. It is a produced as an inactive proenzyme, which is comprised of the active part of the enzyme, the mature form, and a covalently bonded inhibitory pro-region. Activation of the enzyme requires cleavage of the N terminal inhibitory pro-region (staphostatin B) | Defined by 4 residues: GLN:A-203 [auth A-237]CYS:A-209 [auth A-243]HIS:A-306 [auth A-340]ASN:A-326 [auth A-360] | EC: 3.4.22 (PDB Primary Data) |
