4Z9G: Human corticotropin-releasing factor receptor 1

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. Determined by X-ray diffraction at 3.18 Å resolution. Released 29 Jun 2016.

Method: X-ray diffraction
Resolution: 3.18 Å
Organisms: Homo sapiens, Enterobacteria phage RB51
Chains: 3
Atoms: 10,244
Mol. weight: 156.02 kDa
Ligands: 1Q5, OLA
Released: 29 Jun 2016

Explore 4Z9G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Z9G contains 67 α-helices and 18 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	113-143	31
α-helix	145-148	4
α-helix	150-173	24
α-helix	178-182	5
α-helix	186-217	32
α-helix	1003-1007	5
α-helix	1008-1012	5
β-strand	1014-1015	2	1
β-strand	1016	1	2
β-strand	1017-1019	3	1
β-strand	1025-1028	4	1
β-strand	1031-1032	2	1
α-helix	1039-1050	12
β-strand	1057	1	2
α-helix	1060-1080	21
α-helix	1085-1090	6
α-helix	1093-1111	19
α-helix	1116-1122	7
α-helix	1126-1135	10
α-helix	1137-1141	5
α-helix	1143-1155	13
α-helix	1159-222	4
α-helix	228-232	5
α-helix	233-237	5
α-helix	239-252	14
α-helix	257-259	3
α-helix	270-295	26
α-helix	304-330	27
α-helix	340-353	14
α-helix	355-369	15

Chain B: 22 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	114-143	30
α-helix	145-148	4
α-helix	150-174	25
α-helix	178-182	5
α-helix	186-218	33
α-helix	1003-1010	8
β-strand	1014-1015	2	3
β-strand	1016	1	4
β-strand	1017-1019	3	3
β-strand	1025-1028	4	3
β-strand	1031-1034	4	3
α-helix	1039-1050	12
β-strand	1057	1	4
α-helix	1060-1080	21
α-helix	1084-1090	7
α-helix	1093-1111	19
α-helix	1115-1122	8
α-helix	1126-1132	7
α-helix	1138-1141	4
α-helix	1143-1155	13
α-helix	1159-225	7
α-helix	228-232	5
α-helix	233-237	5
α-helix	239-252	14
α-helix	270-296	27
α-helix	304-331	28
α-helix	339-353	15
α-helix	355-369	15

Chain C: 21 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	115-143	29
α-helix	145-148	4
α-helix	150-173	24
α-helix	186-217	32
α-helix	1003-1011	9
β-strand	1014-1015	2	5
β-strand	1016	1	6
β-strand	1017-1019	3	5
β-strand	1025-1028	4	5
β-strand	1031-1032	2	5
α-helix	1039-1050	12
β-strand	1057	1	6
α-helix	1060-1080	21
α-helix	1084-1090	7
α-helix	1093-1111	19
α-helix	1115-1122	8
α-helix	1126-1134	9
α-helix	1138-1141	4
α-helix	1143-1155	13
α-helix	1159-225	7
α-helix	228-232	5
α-helix	233-237	5
α-helix	239-253	15
α-helix	270-296	27
α-helix	304-330	27
α-helix	340-353	14
α-helix	355-369	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Corticotropin-releasing factor receptor 1,Lysozyme,Corticotropin-releasing factor receptor 1	A, B, C	protein	443	Homo sapiens, Enterobacteria phage RB51	C3V2B5, P34998 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>4Z9G_1 Corticotropin-releasing factor receptor 1,Lysozyme,Corticotropin-releasing factor receptor 1 (chains A, B, C)
MEILNEEKKSKVHYHVAAIINYLGHCISLVALLVAFVLFLRARSIRCLRNIIHANLIAAF
ILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTNI
FEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLSVAKSELDKAIGRNSNGVITKDEA
EKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRSALINMVFQMGETGVAGFTNSLRMLQQ
KRWDEAAVNLAKSRWYNQTPNRAKRVIATFRTGTWDAYLTDRLRAWMFICIGWGVPFPII
VAWAIGKLYYDNEKCWAGKRPGVYTDYIYQGPMALVLLINFIFLFNIVRILMTKLRASTT
SETIQARKAVKATLVLLPLLGITYMLAFVNPGEDEVSRVVFIYFNAFLESFQGFFVSVFA
CFLNSEVRSAAAAHHHHHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
1Q5	3,6-dimethyl-N-(pentan-3-yl)-2-(2,4,6-trimethylphenoxy)pyridin-4-amine	C21 H30 N2 O	3
OLA	Oleic acid	C18 H34 O2	10

Water and common crystallization additives (SO4) are not listed.

Primary citation

Decoding Corticotropin-Releasing Factor Receptor Type 1 Crystal Structures. Dore, A.S., Bortolato, A., Hollenstein, K. et al. Curr Mol Pharmacol (2017) 10:334-344. DOI 10.2174/1874467210666170110114727 · PubMed

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