UniProt P00044
Cytochrome c iso-1 (P00044)
Cytochrome c iso-1 (UniProt P00044): 154 experimental structures and 1 predicted model on GenesisL1, 24 ligands bound, 12 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- P00044
- Protein
- Cytochrome c iso-1
- Experimental structures
- 154
- Predicted models
- 1
- Ligands
- 24
- Pockets
- 12 · 3 records with a druggable one
Structures
155 records of P00044 in the MolNFT archive: 154 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1CHH | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CHH | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CHI | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CHI | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CHJ | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CHJ | Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome C | x-ray diffraction | A | — | — |
| 1CIE | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIE | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIF | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIF | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIG | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIG | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIH | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CIH | Structural and functional effects of multiple mutations at distal sites in cytochrome C | x-ray diffraction | A | — | — |
| 1CRG | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRG | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRH | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRH | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRI | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRI | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRJ | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CRJ | The role of a conserved internal water molecule and its associated hydrogen bond network in… | x-ray diffraction | A | — | — |
| 1CSU | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSU | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSV | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSV | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSW | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSW | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSX | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CSX | Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome C | x-ray diffraction | A | — | — |
| 1CTY | Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment | x-ray diffraction | A | — | — |
| 1CTY | Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment | x-ray diffraction | A | — | — |
| 1CTZ | Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment | x-ray diffraction | A | — | — |
| 1CTZ | Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment | x-ray diffraction | A | — | — |
| 1FHB | Three-dimensional solution structure of the cyanide adduct of a MET80ALA variant of saccharomyces… | solution nmr | A | — | — |
| 1FHB | Three-dimensional solution structure of the cyanide adduct of a MET80ALA variant of saccharomyces… | solution nmr | A | — | — |
| 1IRV | Cytochrome C isozyme 1, reduced, mutant with ile 75 replaced by met and cys 102 replaced by thr | x-ray diffraction | A | — | — |
| 1IRV | Cytochrome C isozyme 1, reduced, mutant with ile 75 replaced by met and cys 102 replaced by thr | x-ray diffraction | A | — | — |
| 1IRW | Cytochrome C isozyme 1, reduced, mutant with asn 52 replaced by ala and cys 102 replaced by thr | x-ray diffraction | A | — | — |
| 1IRW | Cytochrome C isozyme 1, reduced, mutant with asn 52 replaced by ala and cys 102 replaced by thr | x-ray diffraction | A | — | — |
| 1KYO | Yeast cytochrome BC1 complex with bound substrate cytochrome C | x-ray diffraction | W | — | — |
| 1KYO | Yeast cytochrome BC1 complex with bound substrate cytochrome C | x-ray diffraction | W | — | — |
| 1LMS | Structural model for an alkaline form of ferricytochrome c | solution nmr | A | — | — |
| 1LMS | Structural model for an alkaline form of ferricytochrome C | solution nmr | A | — | — |
| 1NMI | Solution structure of the imidazole complex of iso-1 cytochrome c | solution nmr | A | — | — |
| 1NMI | Solution structure of the imidazole complex of iso-1 cytochrome C | solution nmr | A | — | — |
| 1RAP | The structure and function of omega loop a replacements in cytochrome C | x-ray diffraction | A | — | — |
| 1RAP | The structure and function of omega loop a replacements in cytochrome C | x-ray diffraction | A | — | — |
| 1RAQ | The structure and function of omega loop a replacements in cytochrome C | x-ray diffraction | A | — | — |
| 1RAQ | The structure and function of omega loop a replacements in cytochrome C | x-ray diffraction | A | — | — |
| 1S6V | Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link | x-ray diffraction | B, D | — | — |
| 1S6V | Structure of a cytochrome C peroxidase-cytochrome C site specific cross-link | x-ray diffraction | B, D | — | — |
| 1U74 | Electron Transfer Complex between cytochrome C and cytochrome C peroxidase | x-ray diffraction | B, D | — | — |
| 1U74 | Electron transfer complex between cytochrome C and cytochrome C peroxidase | x-ray diffraction | B, D | — | — |
| 1YCC | High-resolution refinement of yeast iso-1-cytochrome C and comparisons with other eukaryotic… | x-ray diffraction | A | — | — |
| 1YCC | High-resolution refinement of yeast iso-1-cytochrome C and comparisons with other eukaryotic… | x-ray diffraction | A | — | — |
| 1YFC | Solution nmr structure of a yeast iso-1-ferrocytochrome C | solution nmr | A | — | — |
| 1YFC | Solution NMR structure of a yeast iso-1-ferrocytochrome C | solution nmr | A | — | — |
| 1YIC | The oxidized saccharomyces cerevisiae iso-1-cytochrome C, NMR, 20 structures | solution nmr | A | — | — |
| 1YIC | The oxidized saccharomyces cerevisiae iso-1-cytochrome C, NMR, 20 structures | solution nmr | A | — | — |
95 records more on the page itself.
Ligands
- HEC · Heme C · in 35 records
- SO4 · Sulfate ion · in 14 records
- EVB · sulfonato-calix[8]arene · in 11 records
- 80M · sulfonato-thiacalix[4]arene · in 4 records
- HEM · Protoporphyrin IX containing Fe · in 4 records
- 7AZ · phosphonato-calix[6]arene · in 3 records
- CL · Chloride ion · in 3 records
- 6UZ · omega-undecylenyl-beta-D-maltopyranoside · in 2 records
- 6VJ · Phenyl-trisulfonatocalix[4]arene · in 2 records
- 8TE · p-Methylphosphonatocalix[4]arene · in 2 records
- B4T · mono-PEGylated sulfonatocalix[4]arene · in 2 records
- NO3 · Nitrate ion · in 2 records
- ZN · Zinc ion · in 2 records
- 6VB · Bromo-trisulfonatocalix[4]arene · in 1 record
- B4X · Di-pegylated sulfonatocalix[4]arene · in 1 record
- BR · Bromide ion · in 1 record
- CM5 · 5-cyclohexyl-1-pentyl-beta-D-maltoside · in 1 record
- FWQ · P-sulfonatocalix[6]arene · in 1 record
- L0T · 8-acetamido-2-[[2-[[2-[[2-[[2-[[2-[[2-[(2-carboxy-4-sulfonato-quinolin-8-yl)carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]-4-sulfonato-quinolin-8-yl]carbamoyl]quinoline-4-sulfonate · in 1 record
- LVT · Octa-anionic calix[4]arene · in 1 record
- PO4 · Phosphate ion · in 1 record
- SPM · Spermine · in 1 record
- T8W · 4-[[49,50,51,52,53,54,55,56-octahydroxy-11,17,23,29,35, 41,47-heptakis[(4-sulfonatophenyl)methyl]-5-nonacyclo[43.3.1.13,7.19,13.115,19.121,25.127,31.133, 37.139,43]hexapentaconta-1(49),3,5,7(56),9,11,13(55), 15,17,19(54),21,23,25(53),27,29,31(52),33,35,37(51), 39,41,43(50),45,47-tetracosaenyl]methyl]benzenesulfonate · in 1 record
- ZE7 · 6-cyclohexylhexan-1-ol · in 1 record
Experiment against prediction
- 3TYI chain A against the predicted model P00044: TM-score 1.00, RMSD 0.21 Å
- 3TYI chain A against the predicted model P00044: TM-score 1.00, RMSD 0.21 Å
- 4N0K chain A against the predicted model P00044: TM-score 1.00, RMSD 0.21 Å
- 4N0K chain A against the predicted model P00044: TM-score 1.00, RMSD 0.21 Å
- 4YE1 chain B against the predicted model P00044: TM-score 1.00, RMSD 0.26 Å
- 4YE1 chain B against the predicted model P00044: TM-score 1.00, RMSD 0.26 Å
- 3TYI chain B against the predicted model P00044: TM-score 1.00, RMSD 0.26 Å
- 3TYI chain B against the predicted model P00044: TM-score 1.00, RMSD 0.26 Å
- 6S8Y chain A against the predicted model P00044: TM-score 1.00, RMSD 0.26 Å
- 7MRI chain C against the predicted model P00044: TM-score 0.99, RMSD 0.28 Å
Elsewhere
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