Current Protein Identity:P06850
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1GO9 Monitoring the structural Consequences of Phe12-->D-Phe12 and Leu15-->Aib15 substitution in h/r Corticotropin Releasing Hormone: Implications for Design of CRH antagonists. Deposited 2001-10-20 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
154–194(41 aa)
|
Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 3.8;310 K;Pressure 1
NMR sample composition
34% H2O / 66% TFE
|
Resolution not provided |
| 1GOE Monitoring the structural Consequences of Phe12-->D-Phe12 and Leu15-->Aib15 substitution in h/r Corticotropin Releasing Hormone: Implications for Design of CRH antagonists. Deposited 2001-10-20 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
154–194(41 aa)
|
Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 3.8;310 K;Pressure 1
NMR sample composition
34% H2O / 66% TFE
|
Resolution not provided |
| 3EHT Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1) in complex with CRF Deposited 2008-09-14 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain B
180–194(15 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION;pH 6.25;293 K;PEG 3350, Lithium sulfate, Bis-Tris, pH 6.25, VAPOR DIFFUSION, temperature 293K
|
Resolution 3.40 Å R-free 0.252 |
| 3EHU Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1) in complex with CRF Deposited 2008-09-14 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain C
175–194(20 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | CA CALCIUM ION × 1 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION;pH 6.75;293 K;PEG MME 550, calcium chloride, tert-butanol, Bis-Tris, pH 6.75, VAPOR DIFFUSION, temperature 293K
|
Resolution 1.96 Å R-free 0.256 |
| 3EHU Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1) in complex with CRF Deposited 2008-09-14 | Assembly 2 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain D
175–194(20 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | CA CALCIUM ION × 1 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION;pH 6.75;293 K;PEG MME 550, calcium chloride, tert-butanol, Bis-Tris, pH 6.75, VAPOR DIFFUSION, temperature 293K
|
Resolution 1.96 Å R-free 0.256 |
| 6P9X CRF1 Receptor Gs GPCR protein complex with CRF1 peptide Deposited 2019-06-10 | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count |
Chain P
154–194(41 aa)
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.91 Å |