5GS9: CASTOR1-arginine

Crystal structure of CASTOR1-arginine. Determined by X-ray diffraction at 2.5 Å resolution. Released 28 Sept 2016.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,611
Mol. weight: 150.22 kDa
Ligands: ARG
Released: 28 Sept 2016

Explore 5GS9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GS9 contains 66 α-helices and 71 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: 17 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2-16	15	1
α-helix	17-19	3
α-helix	20-32	13
α-helix	34-36	3
β-strand	41-46	6	1
β-strand	50-56	7	1
α-helix	57-60	4
β-strand	69-71	3	1
β-strand	76-81	6	1
β-strand	93	1	2
α-helix	94-97	4
α-helix	98-102	5
α-helix	103-107	5
β-strand	112-116	5	1
β-strand	121-126	6	1
α-helix	127-129	3
α-helix	130-137	8
β-strand	142-147	6	1
β-strand	150-153	4	1
α-helix	170-172	3
α-helix	174-176	3
β-strand	177-178	2	1
β-strand	184-187	4	1
β-strand	188	1	3
α-helix	191-193	3
α-helix	194-206	13
β-strand	228-233	6	1
β-strand	236-242	7	1
α-helix	243-246	4
β-strand	255	1	3
β-strand	263-268	6	1
α-helix	280-290	11
β-strand	295	1	2
β-strand	296-299	4	1
β-strand	304-309	6	1
α-helix	310-312	3
α-helix	313-320	8

Chain B: 17 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-16	15	4
α-helix	17-23	7
α-helix	24-32	9
α-helix	34-36	3
β-strand	41-46	6	4
β-strand	50-56	7	4
α-helix	57-60	4
β-strand	69-71	3	4
β-strand	76-82	7	4
α-helix	94-97	4
α-helix	98-102	5
α-helix	103-107	5
β-strand	112-116	5	4
β-strand	121-126	6	4
α-helix	127-129	3
α-helix	130-137	8
β-strand	142-147	6	4
β-strand	150-153	4	4
α-helix	174-176	3
β-strand	177-178	2	4
β-strand	183-189	7	4
α-helix	191-197	7
α-helix	198-206	9
β-strand	228-233	6	4
β-strand	236-242	7	4
α-helix	243-246	4
α-helix	250	1
β-strand	255	1	4
β-strand	263-268	6	4
α-helix	280-290	11
β-strand	296-299	4	4
β-strand	304-309	6	4
α-helix	310-312	3
α-helix	313-320	8

Chain C: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-15	14	5
α-helix	17-23	7
α-helix	24-32	9
β-strand	41-46	6	5
β-strand	51-56	6	5
α-helix	57-60	4
β-strand	69-71	3	5
α-helix	75	1
β-strand	76-82	7	5
α-helix	98-102	5
α-helix	103-107	5
β-strand	112-116	5	5
β-strand	121-126	6	5
α-helix	127-129	3
α-helix	130-137	8
β-strand	142-147	6	5
β-strand	150-153	4	5
α-helix	166-168	3
α-helix	170-172	3
β-strand	177-178	2	5
β-strand	184-189	6	5
α-helix	191-197	7
α-helix	198-202	5
α-helix	203-207	5
β-strand	228-233	6	5
β-strand	236-242	7	5
α-helix	243-246	4
α-helix	250	1
β-strand	255	1	5
β-strand	263-268	6	5
α-helix	282-290	9
β-strand	296-299	4	5
β-strand	304-309	6	5
α-helix	310-312	3
α-helix	313-320	8

Chain D: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-16	15	6
α-helix	17-23	7
α-helix	24-32	9
β-strand	41-46	6	6
β-strand	50-56	7	6
α-helix	57-60	4
β-strand	69-71	3	6
β-strand	76-82	7	6
α-helix	98-102	5
α-helix	103-107	5
β-strand	112-116	5	6
β-strand	121-126	6	6
α-helix	127-129	3
α-helix	130-137	8
β-strand	142-147	6	6
β-strand	150-153	4	6
β-strand	177-178	2	6
β-strand	184-188	5	6
α-helix	194-202	9
α-helix	203-207	5
β-strand	228-233	6	6
β-strand	236-242	7	6
α-helix	243-246	4
α-helix	250	1
β-strand	255	1	6
β-strand	263-268	6	6
α-helix	280-290	11
β-strand	296-299	4	6
β-strand	304-309	6	6
α-helix	310-312	3
α-helix	313-320	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GATS-like protein 3	A, B, C, D	protein	337	Homo sapiens	Q8WTX7 (AlphaFold model)

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

>5GS9_1 GATS-like protein 3 (chains A, B, C, D)
MELHILEHRVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGF
KELPPSEFLQVAEATWLVLNVSSHSGAAVQAAGVTKIARSVIAPLAEHHVSVLMLSTYQT
DFILVREQDLSVVIHTLAQEFDIYREVGGEPVPVTRDDSSNGFPRTQHGPSPTVHPIQSP
QNRFCVLTLDPETLPAIATTLIDVLFYSHSTPKEAASSSPEPSSITFFAFSLIEGYISIV
MDAETQKKFPSDLLLTSSSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYIST
FNFDHALVPEDGIGSVIEVLQRRQEGLASLEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ARG	Arginine	C6 H15 N4 O2	4

Primary citation

Structural insight into the arginine-binding specificity of CASTOR1 in amino acid-dependent mTORC1 signaling. Xia, J., Wang, R., Zhang, T. et al. Cell Discov (2016) 2:16035-16035. DOI 10.1038/celldisc.2016.35 · PubMed

Other PDB entries of the same protein (UniProt Q8WTX7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9PDO 1.8 Å, Arginine-bound CASTOR1 from Homo sapiens (GATOR2-inspired update)
5I2C 1.8 Å, Arginine-bound CASTOR1 from Homo sapiens
5GT7 2.05 Å, Crystal Structure of Arg-bound CASTOR1
5GV2 2.06 Å, Crystal structure of Arginine-bound CASTOR1 from Homo sapiens
5GT8 2.8 Å, Crystal Structure of apo-CASTOR1
9KP4 3.08 Å, Crystal structure of human CASTOR1 in apo form
9DX2 3.4 Å, Human GATOR2 complex - CASTOR1 bound state
9LWF 3.41 Å, Cryo-EM structure of dual sensor bound GATOR2 complex
9OTI 3.5 Å, GATOR2 complex bound to arginine sensor CASTOR1
9LVK 3.59 Å, Cryo-EM structure of CASTOR1 bound human GATOR2 complex

Browse structure collections

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