9Q32: RIP1 kinase domain

RIP1 kinase domain in complex with compound 1. Determined by X-ray diffraction at 2.49 Å resolution. Released 12 Nov 2025.

Method: X-ray diffraction
Resolution: 2.49 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,431
Mol. weight: 135.59 kDa
Ligands: A1CNV
Released: 12 Nov 2025

Explore 9Q32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q32 contains 65 α-helices and 42 β-strands across 4 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: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11-12	2	1
α-helix	14-16	3
β-strand	17-21	5	1
β-strand	32-36	5	1
β-strand	40-49	10	1
α-helix	57-68	12
β-strand	75	1	2
β-strand	78-84	7	1
β-strand	87-92	6	1
β-strand	99	1	2
α-helix	100-104	5
α-helix	109-111	3
α-helix	112-131	20
α-helix	141-143	3
β-strand	144-146	3	2
β-strand	152-154	3	2
α-helix	163-169	7
α-helix	195-197	3
α-helix	204-205	2
α-helix	207-223	17
α-helix	234-242	9
α-helix	249-251	3
α-helix	258-267	10
α-helix	272-274	3
α-helix	278-292	15

Chain B: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	11-12	2	3
α-helix	14-16	3
β-strand	17	1	3
β-strand	33-36	4	3
β-strand	40-46	7	3
α-helix	57-68	12
β-strand	72	1	4
β-strand	75	1	4
β-strand	78-83	6	3
β-strand	88-92	5	3
β-strand	98-99	2	4
α-helix	100-105	6
α-helix	112-131	20
α-helix	141-143	3
β-strand	144-146	3	4
β-strand	152-154	3	4
α-helix	163-168	6
α-helix	195-197	3
α-helix	204-205	2
α-helix	207-223	17
α-helix	228-230	3
α-helix	235-243	9
α-helix	249-251	3
α-helix	258-267	10
α-helix	272-274	3
α-helix	276-277	2
α-helix	278-292	15

Chain C: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	9	1
β-strand	10-12	3	5
α-helix	14-16	3
β-strand	17	1	5
β-strand	32-36	5	5
β-strand	40-48	9	5
α-helix	51-53	3
α-helix	54-67	14
β-strand	75	1	6
β-strand	78-83	6	5
β-strand	87-92	6	5
β-strand	98-99	2	6
α-helix	100-107	8
α-helix	112-131	20
α-helix	141-143	3
β-strand	144-146	3	6
β-strand	152-154	3	6
α-helix	163-169	7
α-helix	195-197	3
α-helix	204-205	2
α-helix	207-223	17
α-helix	234-242	9
α-helix	249-251	3
α-helix	258-267	10
α-helix	272-274	3
α-helix	278-292	15

Chain D: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	7
α-helix	14-16	3
β-strand	17	1	7
β-strand	32-36	5	7
β-strand	40-46	7	7
α-helix	57-67	11
β-strand	72	1	8
β-strand	75	1	8
β-strand	78-84	7	7
β-strand	87-92	6	7
β-strand	99	1	8
α-helix	100-104	5
α-helix	109-111	3
α-helix	112-131	20
α-helix	141-143	3
β-strand	144-146	3	8
β-strand	152-154	3	8
α-helix	163-167	5
α-helix	195-197	3
α-helix	204-205	2
α-helix	207-223	17
α-helix	228-230	3
α-helix	235-243	9
α-helix	249-251	3
α-helix	258-267	10
α-helix	272-274	3
α-helix	276-277	2
α-helix	278-288	11
α-helix	289-293	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Receptor-interacting serine/threonine-protein kinase 1	A, B, C, D	protein	296	Homo sapiens	Q13546 (AlphaFold model)

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

>9Q32_1 Receptor-interacting serine/threonine-protein kinase 1 (chains A, B, C, D)
GSMQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNE
ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRI
ILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELRE
VDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLI
MAIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE

Ligands and cofactors

ID	Name	Formula	Copies
A1CNV	methyl 1-[(2,6-dichlorophenyl)methyl]-1H-pyrazole-3-carboxylate	C12 H10 Cl2 N2 O2	4

Primary citation

Discovery of Clinical Candidate GDC-8264, a Novel, Potent and Selective RIP1 Inhibitor for Amelioration of Tissue Damage and the Treatment of Inflammatory Diseases. Patel, S., Chen, H., Varfolomeev, E. et al. J Med Chem (2025) 68:23050-23077. DOI 10.1021/acs.jmedchem.5c01891 · PubMed

Other PDB entries of the same protein (UniProt Q13546 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5ZMZ 1.4 Å, Amyloid core of RIP1
6AC5 1.45 Å, Crystal structure of RIPK1 death domain GlcNAcylated by EPEC effector NleB
4ITJ 1.8 Å, Crystal structure of RIP1 kinase in complex with necrostatin-4
6NW2 2.0 Å, Structure of human RIPK1 kinase domain in complex with compound 11
7FD0 2.0 Å, Crystal Structure of human RIPK1 kinase domain in complex with a novel inhibitor
24IB 2.05 Å, Crystal structure of human RIPK1 kinase domain in complex with compound HR10
9Q31 2.05 Å, RIP1 kinase domain in complex with GDC-8264
6NYH 2.1 Å, Structure of human RIPK1 kinase domain in complex with GNE684
9GTY 2.15 Å, RIPK1 in complex with AZ"320
7FCZ 2.21 Å, Crystal Structure of human RIPK1 kinase domain in complex with a novel inhibitor
5HX6 2.23 Å, Crystal structure of RIP1 kinase with a benzo[b][1,4]oxazepin-4-one
4ITH 2.25 Å, Crystal structure of RIP1 kinase in complex with necrostatin-1 analog

Browse structure collections

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