7QYQ
Crystal structure of a DyP-type peroxidase from Pseudomonas putida
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | F_UNCLASSIFIED | e7qyqA1 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: F_UNCLASSIFIED | ECOD (1.6) |
A | PF20628 | e7qyqA2 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: PF20628 | ECOD (1.6) |
B | F_UNCLASSIFIED | e7qyqB2 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: F_UNCLASSIFIED | ECOD (1.6) |
B | PF20628 | e7qyqB1 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: PF20628 | ECOD (1.6) |
C | F_UNCLASSIFIED | e7qyqC2 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: F_UNCLASSIFIED | ECOD (1.6) |
C | PF20628 | e7qyqC1 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: PF20628 | ECOD (1.6) |
D | F_UNCLASSIFIED | e7qyqD2 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: F_UNCLASSIFIED | ECOD (1.6) |
D | PF20628 | e7qyqD1 | A: a+b two layers | X: Alpha-beta plaits | H: Dimeric alpha+beta barrel (From Topology) | T: Dimeric alpha+beta barrel | F: PF20628 | ECOD (1.6) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF20628 | Dyp-type peroxidase, C-terminal (Dyp_perox_C) | Dyp-type peroxidase, C-terminal | Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
---|---|---|---|---|
Dyp-type peroxidase family protein | - | - |