Ankyrin-1
UniProt P16157 · gene ANK1 · Homo sapiens · 1881 residues
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | cryoem | nmr_structure | nmr_shifts | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|---|---|
| No states defined yet. | ||||||||
Unmapped evidence: 37 of 37 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 1 | 0 |
| RCSB PDB | 21 | 0 |
| SMASH-BIO | 14 | 0 |
Structure
No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.
States and transitions
No states defined.
| State | Basis | Parent | Description |
|---|
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-1N11-1 RCSB PDB | xray | resolution: 2.7 Å | in vitro · -173.15 °C · pH 7.5 · ligands BR, CL D34 REGION OF HUMAN ANKYRIN-R AND LINKER · Ankyrin (chains A) | unmapped |
| EV-PDB-2YQF-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7 Solution structure of the death domain of Ankyrin-1 · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-2YVI-1 RCSB PDB | xray | resolution: 1.92 Å | in vitro · -173.15 °C · pH 8.5 · ligands GOL Crystal structure of a death domain of human ankryn protein · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-3KBT-2 RCSB PDB | xray | resolution: 2.75 Å | in vitro · -173.15 °C · pH 6.5 Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK) · Ankyrin-1 (chains C,D) | unmapped |
| EV-PDB-3KBU-2 RCSB PDB | xray | resolution: 2.75 Å | in vitro · -173.15 °C · pH 6.5 · ligands HG Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK), EMTS derivative · Ankyrin-1 (chains C,D) | unmapped |
| EV-PDB-3UD1-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 7 · ligands EOH Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin · Ankyrin-1 (chains A,B,C) | unmapped |
| EV-PDB-7TW3-3 RCSB PDB | cryoem | resolution: 4.4 Å | in vitro Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell · Ankyrin-1 (chains G) | unmapped |
| EV-PDB-7UZU-1 RCSB PDB | cryoem | resolution: 2.3 Å | in vitro Ankyrin-1 (N-terminal region of membrane binding domain, local refinement from consensus reconstruction; bound to N-terminal peptide from band 3) · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-8CS9-1 RCSB PDB | cryoem | resolution: 2.74 Å | in vitro · ligands AJP, CLR, NAG, PIO, branched: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-8CSL-1 RCSB PDB | cryoem | resolution: 25 Å | in vitro Sub-tomogram averaging of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-8CTE-1 RCSB PDB | cryoem | resolution: 2.9 Å | in vitro · ligands AJP, CLR, NAG, PIO Class 2 of erythrocyte ankyrin-1 complex (Composite map) · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-8CSV-1 RCSB PDB | cryoem | resolution: 2.7 Å | in vitro Local refinement of Anykyrin-1 (N-terminal half of membrane binding domain) in Class 2 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-7V0X-1 RCSB PDB | cryoem | resolution: 3 Å | in vitro Local refinement of ankyrin-1 (C-terminal half), class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains J) | unmapped |
| EV-PDB-7V0S-3 RCSB PDB | cryoem | resolution: 2.5 Å | in vitro · ligands AJP, CLR Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains J) | unmapped |
| EV-PDB-7V0M-1 RCSB PDB | cryoem | resolution: 2.7 Å | in vitro Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A) | unmapped |
| EV-PDB-7V0K-3 RCSB PDB | cryoem | resolution: 2.4 Å | in vitro · ligands AJP, CLR, NAG, PIO, PLC Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map) · Ankyrin-1 (chains H) | unmapped |
| EV-PDB-7UZQ-3 RCSB PDB | cryoem | resolution: 2.17 Å | in vitro · ligands AJP, CLR Local refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinement of all classes · Ankyrin-1 (chains J) | unmapped |
| EV-PDB-7TW6-3 RCSB PDB | cryoem | resolution: 5.6 Å | in vitro Cryo-EM structure of human ankyrin complex (B4P1A1) from red blood cell · Ankyrin-1 (chains G) | unmapped |
| EV-PDB-7TW5-3 RCSB PDB | cryoem | resolution: 5.7 Å | in vitro Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell · Ankyrin-1 (chains G,H) | unmapped |
| EV-PDB-3UD2-1 RCSB PDB | xray | resolution: 2.21 Å | in vitro · -173.15 °C · pH 7 · ligands CL, EOH, NA Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin · Ankyrin-1 (chains A,B,C) | unmapped |
| EV-PDB-3F59-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 6.5 · ligands BR Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin · Ankyrin-1 (chains A,B,C,D) | unmapped |
| EV-BMRB-11390 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 7 Solution structure of the death domain of Ankyrin-1 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-AFDB-AF-P16157-F1 AlphaFold DB | af_prediction | plddt: 69.75 pLDDT | in silico AlphaFold DB prediction AF-P16157-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-1881 | unmapped |
| EV-SMASH-SMFS-000217 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8.5 Nonlinear stiffness of NompC gating spring and its implication in mechanotransduction. · Ankyrin repeats; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000872-r0 SMASH-BIO | force_spectroscopy | molecular_stiffness: 0.7 pN/nm | in vitro Nonlinear compliance of NompC gating spring and its implication in mechanotransduction · Ankyrin repeats; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001694 SMASH-BIO | force_spectroscopy | study_record | in vitro Reconstruction of mechanical unfolding and refolding pathways of proteins with atomic force spectroscopy and computer simulations. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002527-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.35 nm | in vitro · pH 7.2 Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002527-r1 SMASH-BIO | force_spectroscopy | contour_length: 39 nm | in vitro · pH 7.2 Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004379-r0 SMASH-BIO | force_spectroscopy | unbinding_force: 30 pN | in vitro Spectrin-ankyrin interaction mechanics: A key force balance factor in the red blood cell membrane skeleton. · Ankyrin repeats; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-004480 SMASH-BIO | force_spectroscopy | study_record | in vitro Capturing the mechanical unfolding pathway of a large protein with coiled-coil probes. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005095 SMASH-BIO | force_spectroscopy | study_record | in vitro A hot-spot motif characterizes the interface between a designed ankyrin-repeat protein and its target ligand. · Ankyrin repeats; force spectroscopy unspecified; experiment class: membrane_mechanics, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-005201 SMASH-BIO | force_spectroscopy | study_record | in vitro Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding. · Ankyrin repeats; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-005244-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 30 pN | in vitro Mechanical anisotropy of ankyrin repeats. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005261 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005788 SMASH-BIO | force_spectroscopy | study_record | in vitro Fast and forceful refolding of stretched alpha-helical solenoid proteins. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005807 SMASH-BIO | force_spectroscopy | study_record | in vitro Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations. · Ankyrin repeats; force spectroscopy unspecified; experiment class: translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007546 SMASH-BIO | force_spectroscopy | study_record | in vitro Elasticity of the red cell membrane and its relation to hemolytic disorders: an optical tweezers study. · Ankyrin repeats; optical tweezers; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
37 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.