9MEZ: MRAS(GDP)

Crystal structure of MRAS(GDP) bound to LZTR1(Kelch domain). Determined by X-ray diffraction at 2.8 Å resolution. Released 10 Sept 2025.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 10
Atoms: 19,477
Mol. weight: 289.62 kDa
Ligands: GDP, MG, MLA
Released: 10 Sept 2025

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

Secondary structure: helices and β-sheets

9MEZ contains 88 α-helices and 251 β-strands across 10 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: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	1
α-helix	26-35	10
β-strand	48-56	9	1
β-strand	59-67	9	1
α-helix	74-75	2
α-helix	76-84	9
β-strand	87-93	7	1
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	1
α-helix	138-148	11
β-strand	152-154	3	1
β-strand	156	1	2
α-helix	161	1
β-strand	162	1	2
α-helix	164-176	13

Chain B: 9 helices, 43 β-strands

Element	Residues	Length	Sheet
β-strand	54-57	4	3
α-helix	58-61	4
β-strand	68	1	4
β-strand	69	1	5
β-strand	72-76	5	5
β-strand	79-86	8	5
β-strand	91-99	9	5
β-strand	104-107	4	5
α-helix	108-109	2
β-strand	111	1	6
α-helix	115-116	2
β-strand	118-119	2	7
β-strand	122-126	5	6
β-strand	129-133	5	6
β-strand	136-139	4	7
β-strand	144-148	5	7
β-strand	149	1	8
β-strand	152-156	5	6
β-strand	161-164	4	6
α-helix	170-174	5
β-strand	175	1	8
β-strand	176	1	9
β-strand	179-183	5	9
β-strand	186-193	8	9
β-strand	198-206	9	9
β-strand	215-217	3	9
β-strand	221-222	2	10
α-helix	224-226	3
β-strand	228	1	9
β-strand	229	1	11
β-strand	233-236	4	10
β-strand	239-243	5	10
β-strand	246	1	11
α-helix	248-250	3
β-strand	255-259	5	10
β-strand	264-267	4	10
α-helix	273-275	3
α-helix	277-283	7
β-strand	285	1	12
β-strand	288-291	4	13
β-strand	295-299	5	13
β-strand	302	1	12
β-strand	311-315	5	13
β-strand	320-323	4	13
α-helix	384-387	4
β-strand	389	1	14
β-strand	392-396	5	3
β-strand	399-403	5	3
β-strand	406-407	2	14
β-strand	411-412	2	14
β-strand	413	1	4
β-strand	416-420	5	3

Chains C and E: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	15
α-helix	26-35	10
β-strand	48-55	8	15
β-strand	60-67	8	15
α-helix	74-75	2
α-helix	76-84	9
β-strand	87-93	7	15
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	15
α-helix	131-133	3
α-helix	138-148	11
β-strand	152-154	3	15
β-strand	156	1	16
α-helix	161	1
β-strand	162	1	16
α-helix	164-176	13

Chain D: 9 helices, 43 β-strands

Element	Residues	Length	Sheet
β-strand	54-57	4	17
α-helix	58-61	4
β-strand	68	1	18
β-strand	69	1	19
β-strand	72-76	5	19
β-strand	79-86	8	19
β-strand	91-99	9	19
β-strand	104-107	4	19
α-helix	108-109	2
β-strand	111	1	20
α-helix	113-116	4
β-strand	118-119	2	21
β-strand	122-126	5	20
β-strand	129-133	5	20
β-strand	136-139	4	21
β-strand	144-148	5	21
β-strand	149	1	22
β-strand	152-156	5	20
β-strand	161-164	4	20
α-helix	170-174	5
β-strand	175	1	22
β-strand	176	1	23
β-strand	179-183	5	23
β-strand	186-193	8	23
β-strand	198-206	9	23
β-strand	215-217	3	23
β-strand	221-222	2	24
α-helix	224-226	3
β-strand	228	1	23
β-strand	229	1	25
β-strand	233-236	4	24
β-strand	239-243	5	24
β-strand	246	1	25
α-helix	248-250	3
β-strand	255-259	5	24
β-strand	264-267	4	24
α-helix	277-283	7
β-strand	285	1	26
β-strand	288-291	4	27
β-strand	295-299	5	27
β-strand	302	1	26
β-strand	311-315	5	27
β-strand	320-323	4	27
α-helix	324-327	4
α-helix	384-387	4
β-strand	389	1	28
β-strand	392-396	5	17
β-strand	399-403	5	17
β-strand	406-407	2	28
β-strand	411-412	2	28
β-strand	413	1	18
β-strand	416-420	5	17

Chain F: 9 helices, 44 β-strands

Element	Residues	Length	Sheet
β-strand	54-57	4	31
α-helix	58-59	2
β-strand	68	1	32
β-strand	69	1	33
β-strand	72-76	5	33
β-strand	79-86	8	33
β-strand	91-99	9	33
β-strand	104-107	4	33
α-helix	108-109	2
β-strand	111	1	34
α-helix	113-116	4
β-strand	118-119	2	35
β-strand	122-126	5	36
β-strand	129-133	5	36
β-strand	136-139	4	35
β-strand	144-148	5	35
β-strand	149	1	37
β-strand	152-156	5	36
β-strand	161	1	34
β-strand	162-164	3	36
α-helix	170-174	5
β-strand	175	1	37
β-strand	176	1	38
β-strand	179-183	5	38
β-strand	186-193	8	38
β-strand	198-206	9	38
β-strand	215-217	3	38
β-strand	221-222	2	39
α-helix	224-226	3
β-strand	228	1	38
β-strand	229	1	40
β-strand	233-236	4	39
β-strand	239-243	5	39
β-strand	246	1	40
α-helix	248-250	3
β-strand	255-259	5	39
β-strand	264-268	5	39
α-helix	269	1
α-helix	277-283	7
β-strand	285	1	41
β-strand	288-291	4	42
β-strand	295-299	5	42
β-strand	302	1	41
β-strand	311-315	5	42
β-strand	320-323	4	42
α-helix	384-387	4
β-strand	389	1	43
β-strand	392-396	5	31
β-strand	399-403	5	31
β-strand	406-407	2	43
β-strand	411-412	2	43
β-strand	413	1	32
β-strand	416-420	5	31

Chain G: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	44
α-helix	26-35	10
β-strand	49-56	8	44
β-strand	59-67	9	44
α-helix	74-75	2
α-helix	76-84	9
β-strand	87-93	7	44
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	44
α-helix	138-147	10
β-strand	152-154	3	44
β-strand	156	1	45
α-helix	161	1
β-strand	162	1	45
α-helix	164-176	13

Chain H: 11 helices, 43 β-strands

Element	Residues	Length	Sheet
β-strand	54-57	4	46
α-helix	58-61	4
β-strand	68	1	47
β-strand	69	1	48
β-strand	72-76	5	48
β-strand	79-86	8	48
β-strand	91-99	9	48
β-strand	104-107	4	48
α-helix	108-109	2
β-strand	111	1	49
α-helix	113-116	4
β-strand	118-119	2	50
β-strand	122-126	5	49
β-strand	129-133	5	49
β-strand	136-139	4	50
β-strand	144-148	5	50
β-strand	149	1	51
β-strand	152-156	5	49
β-strand	161-164	4	49
α-helix	170-174	5
β-strand	175	1	51
β-strand	176	1	52
β-strand	179-183	5	52
β-strand	186-193	8	52
β-strand	198-206	9	52
β-strand	216-217	2	52
β-strand	221-222	2	53
α-helix	224-226	3
β-strand	228	1	52
β-strand	229	1	54
β-strand	233-236	4	53
β-strand	239-243	5	53
β-strand	246	1	54
α-helix	248-250	3
β-strand	255-259	5	53
β-strand	264-267	4	53
α-helix	268-269	2
α-helix	273-275	3
α-helix	278-283	6
β-strand	285	1	55
β-strand	288-291	4	56
β-strand	295-299	5	56
β-strand	302	1	55
β-strand	311-315	5	56
β-strand	320-324	5	56
α-helix	325-327	3
α-helix	384-387	4
β-strand	389	1	57
β-strand	392-396	5	46
β-strand	399-403	5	46
β-strand	406-407	2	57
β-strand	411-412	2	57
β-strand	413	1	47
β-strand	416-420	5	46

Chain I: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	58
α-helix	26-35	10
β-strand	49-55	7	58
β-strand	60-67	8	58
α-helix	74-75	2
α-helix	76-84	9
β-strand	87-93	7	58
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	58
α-helix	138-148	11
β-strand	152-154	3	58
β-strand	156	1	59
α-helix	161	1
β-strand	162	1	59
α-helix	164-176	13

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related protein M-Ras	A, C, E, G, I	protein	182	Homo sapiens	O14807 (AlphaFold model)
Leucine-zipper-like transcriptional regulator 1	B, D, F, H, J	protein	322	Homo sapiens	Q8N653 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I), FASTA

>9MEZ_1 Ras-related protein M-Ras (chains A, C, E, G, I)
GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQ
WAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESF
PMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQI
PE

Sequence of entity 2 (B, D, F, H, J), FASTA

>9MEZ_2 Leucine-zipper-like transcriptional regulator 1 (chains B, D, F, H, J)
GTVHRWRRLPPCDEFVGARRSKHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWCRA
FTTGTPPAPRYHHSAVVYGSSMFVFGGYTGDIYSNSNLKNKNDLFEYKFATGQWTEWKIE
GRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWTIGLQDRELTCWEEVAQSGEIPPSC
CNFPVAVCRDKMFVFSGQSGAKITNNLFQFEFKDKTWTRIPTEHLLRGSPPPPQRRYGHT
MVAFDRHLYVFGGAADNTLPNELHCYDVDFQTWEVVQPSSDSELPSGRLFHAAAVISDAM
YIFGGTVDNNIRSGEMYRFQFS

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	5
MG	Magnesium ion	Mg	5
MLA	Malonic acid	C3 H4 O4	3

Water and common crystallization additives (FMT, ACT) are not listed.

Primary citation

Structural basis for LZTR1 recognition of RAS GTPases for degradation. Dharmaiah, S., Bonsor, D.A., Mo, S.P. et al. Science (2025) 389:1112-1117. DOI 10.1126/science.adv7088 · PubMed

Other PDB entries of the same protein (UniProt O14807 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9O0P 1.5 Å, Crystal structure of GDP-bound mutant MRAS in complex with MRTX1133
9O0Q 1.9 Å, Crystal structure of GMPPNP-bound mutant MRAS in complex with MRTX1133
7TXH 1.95 Å, Human MRas Q71R in complex with human Shoc2 LRR domain M173I and human PP1Ca
9C1A 1.96 Å, Crystal structure of GDP-bound human M-RAS protein in crystal form I
9B4R 2.1 Å, Crystal structure of MRAS bound to GMPPNP
7TVF 2.17 Å, Crystal structure of the SHOC2-MRAS-PP1CA (SMP) complex to a resolution of 2.17 Angstrom
9C1B 2.27 Å, Crystal structure of GDP-bound human M-RAS protein in crystal form II
9B4T 2.75 Å, Crystal structure of the MRAS-p110alpha complex
7UPI 2.89 Å, Cryo-EM structure of SHOC2-PP1c-MRAS holophosphatase complex
7SD0 2.95 Å, Cryo-EM structure of the SHOC2:PP1C:MRAS complex

Browse structure collections

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