Table 1. Summary of published pseudokinase crystal structures.

Abbreviations: P-PCP, β,γ-methyleneadenosine 5′-triphosphate; AMP-PN, AMP phosphoramidate. *Crystallized with surface mutations (W659A, W777A, F794H). †Inferred from biochemical data or close homology to published structures showing the nt-binding mode. ‡Can be made cation-dependent with four point mutations [83]. ^§Mutated as explained in [77]. ^¶Not identical with ROP2 sequence in 2W1Z.

	Crystal structures
Protein	PDB ID	Species	Ligand	Complex	Kd for ATP	Binding mode	Other
KSR2	2Y4I	Homo sapiens	ATP + Mg	MEK1	Unknown	1 cation	Active, phosphorylates MEK1 [4]
HER3	4OTW	H. sapiens	Bosutinib	–	10−6 M [5]	1 cation	Active, autophosphorylates its own intracellular region, when immobilized on vesicles [5]
	4RIW	H. sapiens	AMP-PNP + Mg	EGFR KD (V624R, F973A, L977A)
	4RIX (Q709R)	H. sapiens	AMP-PNP + Mg	EGFR KD (V624R, F973A, L977A)
	4RIY (E909G)	H. sapiens	AMP-PNP + Mg	EGFR KD (V624R, F973A, L977A)
	3KEX	H. sapiens	AMP-PNP + Mg	–
	3LMG	H. sapiens	AMP-PNP + Mg	–
TYK2 JH2	3ZON	H. sapiens	IKK1	–	10−5 M [37]	1 cation	Inactive [37]
	4WOV	H. sapiens	BMS-066	–
	4OLI	H. sapiens	Inhibitor 7012	JH2-JH1 (D1023N)
	5C03	H. sapiens	ATPγS + Mg	–
	5C01	H. sapiens	Pyrazine inhibitor	–
JAK2 JH2	4FVP*	H. sapiens	–	–	10−6 M [6,45]	1 cation	Active, autophosphorylates on S523 and Y570 [6]
	4FVQ*	H. sapiens	ATP + Mg	–
	4FVR (V617F)*	H. sapiens	ATP + Mg	–
JAK1 JH2	4L00	H. sapiens	–	–	10−6 M [45]	1 cation†	Inactive [65]
	4L01 (V658F)	H. sapiens	–	–
MLKL	4BTF	Mus musculus	–	–	10−5 M (TSA) [26]	No cation† [9,25,26]	Inactive [25]
	4MWI	H. sapiens	–	–
	4M67	H. sapiens	–	–
	4M68	M. musculus	–	–
	4M69	M. musculus	–	RIP3 KD
STRADα	3GNI	H. sapiens	ATP	MO25	10−4–10−6 M [39,82]	No cation [9]	Inactive [140]
	2WTK	H. sapiens	AMP-PNP	MO25 + LKB1
VRK3	2JII	H. sapiens	–	–	None	N/A	Inactive
ILK	3KMW	H. sapiens	ATP + Mg	α-Parvin	10−6 M [34]	1 cation	Inactive [34,40]
	3KMU	H. sapiens	–	α-Parvin
	3REP	H. sapiens	ATP + Mn	α-Parvin
CASK	3C0G	H. sapiens	3′-AMP	–	10−3 M [7,9]	No cation	Active, cations inhibit binding and activity. [7,24,83]
	3C0I	H. sapiens	3′-AMP	–
	3C0H	H. sapiens	AMP-PNP (only AMP visible)	–
	3TAC	H. sapiens	–	Liprin-α2
	3MFS (4M)‡	H. sapiens	AMP-PNP	–
	3MFU (4M)‡	H. sapiens	AMP-PNP + Mn	–
	3MFT (4M)‡	H. sapiens	–	–
	3MFR (4M)‡	H. sapiens	–	–
ROR2	3ZZW	H. sapiens	–	–	None [55]	N/A	Inactive [55,102]
	4GT4	H. sapiens	–	–
BIR2	4L68	Arabidopsis thaliana	–	–	None [94]	N/A	Inactive [94]
BSK8	4I92	A. thaliana	–	–	Unknown	1 cation	Inactive [76]
	4I93	A. thaliana	–	–
	4I94	A. thaliana	AMP-PNP	–
Titin	4JNW	H. sapiens	–	–	10−4 M [113]	Unknown	Disputed [112–114]
	1TKI	H. sapiens	–	–
PAN3	4CYI	Chaetomium thermophilum	ATP + Mg	–	Unknown, but probably rather high affinity [78]	1 cation	Unknown, physiological role of PKD is to shuttle polyribonucleotides to PAN2 [81]
	4CYJ	C. thermophilum	ATP + Mg	PAN2
	4CZY	Neurospora crassa	AMP-PNP + Mg	PAN2
	4BWK	N. crassa	ATPγS	–
	4BWX§	N. crassa	ATPγS + Mg
	4BWP	Drosophila melanogaster	AMP-PN	–
	4XR7	Saccharomyces cerevisiae	–	PAN2
ROP2	2W1Z	T. gondii	–	–	None [43]	N/A	Inactive [43]
	3DZO¶	T. gondii	Mg	–
ROP5B	3Q5Z	T. gondii	–	–	Unknown	2 cations	Inactive [110]
	3Q60	T. gondii	ATP + Mg	–
	4LV5	T. gondii	ADP	IRGa6 (M. musculus)
ROP5C	4LV8	T. gondii	ADP + Mg	IRGa6 (M. musculus)	Unknown	1 cation	Unknown
ROP8	3BYV	T. gondii	Mg	–	Unknown	Unknown	Unknown
RNase L	4O1O	Sus scrofa	–	2-5A	10−3 M [53]	2 cations	Inactive [52–54]
	4O1P	S. scrofa	AMP-PNP + Mg	2-5A
	4OAU	H. sapiens	ADP + Mg	2-5A
	4OAV	H. sapiens	AMP-PCP + Mg	RNA + pUp
WNK1	4Q2A	Rattus norvegicus	Br	–	Unknown	Unknown	Active [124]
	3FPQ	R. norvegicus	–	–
	4PWN	H. sapiens	–	–
MviN	3OTV	Mycobacterium tuberculosis	–	–	None [47]	Unknown	Inactive [47]
	3OUK	M. tuberculosis	–	–
	3OUN	M. tuberculosis	–	FhaA
	3UQC	M. tuberculosis	–	–
ADCK3	4PED	H. sapiens	–	–	Binds preferentially ADP [108]	Unknown	Inactive, can be activated with a single Gly-rich loop mutation [108]