Current Protein Identity:P34998
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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 |
|---|---|---|---|---|---|---|---|
| 2L27 NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist Deposited 2010-08-12 | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
25–108(84 aa)
Fragment:residues 28-111
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 6.5;308 K;Ionic strength (raw mmCIF value) 0.3;Pressure ambient
NMR sample composition
0.3 mM [U-100% 13C; U-100% 15N] ECD1-CRF-R1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition
0.4 mM [U-100% 13C; U-100% 15N] Alpha Helical CRF, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 3EHS Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1) Deposited 2008-09-14 | Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
24–119(96 aa)
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION;pH 4.7;293 K;NaCl, sucrose, sodium acetate, pH 4.7, vapor diffusion, temperature 293K
|
Resolution 2.76 Å R-free 0.240 |
| 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 A
24–119(96 aa)
|
Mutation:F(-257)E | 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 A
24–119(96 aa)
|
Mutation:A(-25)E | 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 B
24–119(96 aa)
|
Mutation:A(-25)E | 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 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
104–220(117 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
Chain A
224–373(150 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLA OLEIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 SO4 SULFATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Assembly 2 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain B
104–220(117 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
Chain B
224–373(150 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 SO4 SULFATE ION × 3 PGW (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 3 1PE PENTAETHYLENE GLYCOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4K5Y Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 Deposited 2013-04-15 | Assembly 3 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain C
104–220(117 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
Chain C
224–373(150 aa)
Fragment:UNP P34998 RESIDUES 104-220, UNP P00720 RESIDUES 2-161, UNP P34998 RESIDUES 224-373
|
Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a Mutation:v120a, l144a, w156a, s160a, n40s, a41v, c54s, c97s, t151a, k228a, f260a, i277a, y309a, f330a, s349a, y363a | 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 OLA OLEIC ACID × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (v/v) PEG 400, 0.2M lithium sulphate, 0.1M sodium citrate 5.5, Lipidic Cubic Phase, temperature 295.6K
|
Resolution 2.98 Å R-free 0.265 |
| 4Z9G Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 in a hexagonal setting with translational non-crystallographic symmetry Deposited 2015-04-10 | Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
103–220(118 aa)
Chain A
252–401(150 aa)
|
Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; | OLA OLEIC ACID × 3 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 SO4 SULFATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (V/V) PEG 400, 0.2M LITHIUM SULPHATE, 0.1M SODIUM CITRATE 5.5
|
Resolution 3.18 Å R-free 0.289 |
| 4Z9G Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 in a hexagonal setting with translational non-crystallographic symmetry Deposited 2015-04-10 | Assembly 2 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain B
103–220(118 aa)
Chain B
252–401(150 aa)
|
Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; | OLA OLEIC ACID × 3 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (V/V) PEG 400, 0.2M LITHIUM SULPHATE, 0.1M SODIUM CITRATE 5.5
|
Resolution 3.18 Å R-free 0.289 |
| 4Z9G Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 in a hexagonal setting with translational non-crystallographic symmetry Deposited 2015-04-10 | Assembly 3 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain C
103–220(118 aa)
Chain C
252–401(150 aa)
|
Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; Mutation:;V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A,V120A, L144A, W156A, S160A, N1040S, A1041V, C1054S, C1097S, T1151A, S222L, K228A, F260A, I277A, Y309A, F330A, S349A, Y363A ; | OLA OLEIC ACID × 4 1Q5 3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine × 1 SO4 SULFATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
LIPIDIC CUBIC PHASE;pH 5.5;295.6 K;30% (V/V) PEG 400, 0.2M LITHIUM SULPHATE, 0.1M SODIUM CITRATE 5.5
|
Resolution 3.18 Å R-free 0.289 |
| 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 R
23–415(393 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 |
| 6PB0 Cryo-EM structure of Urocortin 1-bound Corticotropin-releasing factor 1 receptor in complex with Gs protein and Nb35 Deposited 2019-06-12 | Assembly 1 Insufficient information Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count |
Chain R
24–398(375 aa)
|
Not recorded | CLR CHOLESTEROL × 5 PLM PALMITIC ACID × 7 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |