HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI
External Resource: Annotation
- Domain Annotation: SCOP/SCOPe Classification
- Domain Annotation: SCOP2 Classification
- Domain Annotation: ECOD Classification
- Domain Annotation: CATH
- Protein Family Annotation
- Gene Ontology: Gene Product Annotation
- InterPro: Protein Family Classification
- Pharos: Disease Associations
- Structure Motif: Primary M-CSA Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1bzca_ | Alpha and beta proteins (a/b) | (Phosphotyrosine protein) phosphatases II | (Phosphotyrosine protein) phosphatases II | Higher-molecular-weight phosphotyrosine protein phosphatases | Tyrosine phosphatase | human (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Y_phosphatase | e1bzcA1 | A: a/b three-layered sandwiches | X: Flavodoxin-like | H: Flavoproteins/Phosphotyrosine protein phosphatases-like | T: (Phosphotyrosine protein) phosphatases II | F: Y_phosphatase | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.90.190.10 | Alpha Beta | Alpha-Beta Complex | Protein-Tyrosine Phosphatase | Chain A | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00102 | Protein-tyrosine phosphatase (Y_phosphatase) | Protein-tyrosine phosphatase | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR016130 | Protein-tyrosine phosphatase, active site | Active Site | |
IPR051985 | Non-receptor type tyrosine-specific phosphatase | Family | |
IPR012265 | Protein-tyrosine phosphatase, non-receptor type-1/2 | Family | |
IPR003595 | Protein-tyrosine phosphatase, catalytic | Domain | |
IPR029021 | Protein-tyrosine phosphatase-like | Homologous Superfamily | |
IPR000242 | Tyrosine-specific protein phosphatase, PTPase domain | Domain | |
IPR000387 | Tyrosine-specific protein phosphatases domain | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Chains | Drug Target | Associated Disease |
---|---|---|
P18031 | :
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
protein-tyrosine-phosphatase non-receptor type 1 M-CSA #469 | Protein tyrosine phosphatases catalyse the removal of phosphoryl groups from tyrosine residues in proteins. They play important roles in the control of biological processes such as cell cycles and signal transduction pathways. | Defined by 5 residues: ASP:A-181CYS:A-215ARG:A-221SER:A-222GLN:A-262 | EC: 3.1.3.48 (PDB Primary Data) |