Cytochrome c
UniProt P62894 · gene CYCS · Bos taurus · 105 residues
34evidence items
0mapped to a state
0states
6techniques
5sources
0conflicts
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_shifts | saxs_sans | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|---|---|
| No states defined yet. | ||||||||
Unmapped evidence: 34 of 34 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 26 | 0 |
| RCSB PDB | 5 | 0 |
| SASBDB | 1 | 0 |
| SMASH-BIO | 1 | 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-2YBB-33 RCSB PDB | cryoem | resolution: 19 Å | in vitro · ligands CA, CDL, CU, FES, FMN, HEA, HEC, HEM, MG, NAI, SF4, SMA, UQ1, ZN Fitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876) · CYTOCHROME C (chains Y) | unmapped |
| EV-PDB-3J2T-2 RCSB PDB | cryoem | resolution: 9.5 Å | in vitro · ligands ATP, HEM An improved model of the human apoptosome · Cytochrome c (chains H,I,J,K,L,M,N) | unmapped |
| EV-PDB-6FF5-1 RCSB PDB | xray | resolution: 1.74 Å | in vitro · -173.15 °C · ligands HEC, NO3, SO4 X-ray structure of bovine heart cytochrome c at high ionic strength · Cytochrome c (chains A) | unmapped |
| EV-PDB-5JUY-2 RCSB PDB | cryoem | resolution: 4.1 Å | in vitro · ligands DTP, HEC Active human apoptosome with procaspase-9 · Cytochrome c (chains H,I,J,K,L,M,N) | unmapped |
| EV-PDB-2B4Z-1 RCSB PDB | xray | resolution: 1.5 Å | in vitro · pH 7 · ligands HEM Crystal structure of cytochrome C from bovine heart at 1.5 A resolution. · Cytochrome c (chains A) | unmapped |
| EV-BMRB-1108 BMRB | nmr_shifts | chemical_shift | in vitro · 35.85 °C · pH 6.68 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1109 BMRB | nmr_shifts | chemical_shift | in vitro · 35.85 °C · pH 6.9 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1110 BMRB | nmr_shifts | chemical_shift | in vitro · 35.85 °C · pH 6.7 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1111 BMRB | nmr_shifts | chemical_shift | in vitro · 10.85 °C · pH 6.7 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1112 BMRB | nmr_shifts | chemical_shift | in vitro · 35.85 °C · pH 6.7 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1114 BMRB | nmr_shifts | chemical_shift | in vitro · 10.85 °C · pH 6.7 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1116 BMRB | nmr_shifts | chemical_shift | in vitro · 35.85 °C · pH 5.5 Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-1170 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 7.2 Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-cytochrome c and Horse Cytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-1404 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 5.5 A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c · BMRB data: 13C chemical shifts | unmapped |
| EV-BMRB-17847 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C · pH 6 Backbone 1H, 13C, and 15N chemical shift assignments of oxidized horse heart cytochrome c · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17848 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C · pH 6 Backbone 1H, 13C, and 15N chemical shift assignments of reduced horse heart cytochrome c · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-2366 BMRB | nmr_shifts | chemical_shift | in vitro · 56.85 °C · pH 7 Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-2367 BMRB | nmr_shifts | chemical_shift | in vitro · 56.85 °C · pH 7 Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-2368 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 7 Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-243 BMRB | nmr_shifts | chemical_shift | in vitro · 39.85 °C · pH 5.7 Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-244 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 5.7 Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-274 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 5.7 Proton Resonance Assignments of Horse Ferricytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-285 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 5.7 Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-286 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 5.7 Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-316 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C · pH 6.8 Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-317 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C · pH 6.8 Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-4189 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 7 Solution Structure of Reduced Horse Heart Cytochrome c · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-4805 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C 1H, 13C and 15N chemical shifts of bovine ferric cytochrome b5 in complex with horse heart ferric cytochrome c · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-4808 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C 1H, 13C and 15N chemical shifts of bovine ferrous cytochrome b5 in complex with horse heart ferrous cytochrome c · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-4809 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C 1H, 13C and 15N chemical shifts of bovine ferrous cytochrome b5-N17D in complex with horse heart ferrous cytochrome c · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-4810 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C 1H, 13C and 15N chemical shifts of bovine ferric cytochrome b5 in complex with horse heart ferric cytochrome c · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-SASBDB-SASDCS8 SASBDB | saxs_sans | radius_of_gyration: 1.34 nm ± 0.07 | in vitro · 20 °C · pH 7.4 A high flux setup for millisecond-scale small-angle X-ray scattering studies on macromolecular solutions · Cytochrome C | unmapped |
| EV-AFDB-AF-P62894-F1 AlphaFold DB | af_prediction | plddt: 97.81 pLDDT | in silico AlphaFold DB prediction AF-P62894-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-105 | unmapped |
| EV-SMASH-SMFS-006154 SMASH-BIO | force_spectroscopy | study_record | in vitro Probing the recognition specificity of a protein molecularly imprinted polymer using force spectroscopy. · Cytochrome c; afm smfs; experiment class: force_generation_polymerization, receptor_ligand_adhesion | unmapped |
Conflicts
No conflicts found among comparable evidence.
33 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.