7TZG: Human LAG3

Structure of human LAG3 in complex with antibody single-chain variable fragment. Determined by X-ray diffraction at 3.71 Å resolution. Released 11 May 2022.

Method: X-ray diffraction
Resolution: 3.71 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,716
Mol. weight: 141.84 kDa
Ligands: NAG
Released: 11 May 2022

Explore 7TZG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7TZG contains 19 α-helices and 105 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: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	1
β-strand	13-14	2	2
β-strand	20-27	8	1
α-helix	31-33	3
β-strand	36-41	6	3
β-strand	47-53	7	3
β-strand	61-62	2	3
β-strand	70-75	6	1
β-strand	80-85	6	1
α-helix	90-92	3
β-strand	94-100	7	3
β-strand	106	1	4
β-strand	114	1	3
β-strand	118-120	3	3
β-strand	121-122	2	2
β-strand	143-145	3	5
β-strand	149-151	3	6
β-strand	158-164	7	5
β-strand	172-177	6	6
β-strand	184-187	4	6
β-strand	193	1	6
α-helix	194	1
β-strand	201-206	6	5
β-strand	209-214	6	5
α-helix	219-221	3
β-strand	224-229	6	6
β-strand	232	1	7
β-strand	237	1	6
β-strand	241-244	4	6

Chain B: 3 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	8
β-strand	12-14	3	9
β-strand	20-27	8	8
β-strand	36-41	6	9
β-strand	47-53	7	9
β-strand	60-62	3	9
β-strand	70-75	6	8
β-strand	80-85	6	8
α-helix	90-92	3
β-strand	94-101	8	9
β-strand	106	1	10
β-strand	111-114	4	9
β-strand	115	1	8
β-strand	118-122	5	9
β-strand	143-145	3	11
β-strand	149-152	4	12
β-strand	158-168	11	11
β-strand	172-177	6	12
β-strand	183-188	6	12
β-strand	192-193	2	12
α-helix	194	1
β-strand	201-214	14	11
α-helix	219-221	3
β-strand	224-229	6	12
β-strand	237	1	12
β-strand	241-245	5	12

Chain C: 8 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	60-61	2
β-strand	62-66	5	13
α-helix	136-138	3
β-strand	146-151	6	13
β-strand	158-162	5	13
β-strand	171-173	3	14
β-strand	179	1	15
β-strand	185-189	5	14
α-helix	196	1
β-strand	197-203	7	16
α-helix	211-213	3
β-strand	221-222	2	14
β-strand	225-228	4	14
α-helix	233-235	3
β-strand	237-245	9	16
β-strand	249-257	9	16
β-strand	259	1	15
β-strand	268-273	6	17
β-strand	278-280	3	18
β-strand	295-299	5	17
β-strand	308-310	3	17
β-strand	312	1	19
β-strand	315	1	19
β-strand	318-320	3	18
α-helix	325-327	3
β-strand	329-336	8	17
β-strand	341-355	15	17
β-strand	365-371	7	17
β-strand	379-383	5	20
β-strand	390	1	10
α-helix	391-392	2
β-strand	393-394	2	20
β-strand	398-400	3	17
α-helix	402-407	6
β-strand	411-416	6	20
β-strand	419-425	7	20

Chain D: 4 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	43	1	21
β-strand	60-66	7	22
β-strand	103	1	22
β-strand	133	1	21
β-strand	146-152	7	22
β-strand	159-161	3	22
β-strand	170-173	4	23
β-strand	179	1	24
β-strand	185-190	6	23
β-strand	199-203	5	25
β-strand	220-221	2	23
β-strand	225-228	4	23
α-helix	233-236	4
β-strand	239-244	6	25
β-strand	251-255	5	25
β-strand	259	1	24
β-strand	268-273	6	26
β-strand	280	1	27
α-helix	283-285	3
α-helix	292-293	2
β-strand	296-299	4	26
β-strand	318	1	27
β-strand	329-335	7	26
β-strand	342-355	14	26
β-strand	367-371	5	26
β-strand	378-384	7	28
β-strand	390	1	4
α-helix	391	1
β-strand	392	1	7
β-strand	393-394	2	28
β-strand	397-398	2	26
β-strand	410-416	7	28
β-strand	419-425	7	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
scFvF7	A, B	protein	248	Homo sapiens
Lymphocyte activation gene 3 protein	C, D	protein	408	Homo sapiens	P18627 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7TZG_1 scFvF7 (chains A, B)
MAQVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMNWVRQAPGKGLEWVSGISAGGTGT
YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKDQDGGKKTDAFDIWGQGTMV
TVSSGGGGSGGGGSGGGGSDIVMTQSPSLLSASVGDRVTITCRASQGINYYLAWYQQKPG
KAPKLLIYAASTLQSGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCQQTGYYPLTFGPG
TKVDIAAA

Sequence of entity 2 (C, D), FASTA

>7TZG_2 Lymphocyte activation gene 3 protein (chains C, D)
LQPGAEVPVVWAQEGAPAQLPCSPTIPLQDLSLLRRAGVTWQHQPDSGPPAAAPGHPLAP
GPHPAAPSSWGPRPRRYTVLSVGPGGLRSGRLPLQPRVQLDERGRQRGDFSLWLRPARRA
DAGEYRAAVHLRDRALSCRLRLRLGQASITASPPGSLRASDWVILNCSFSRPDRPASVHW
FRNRGQGRVPVRESPHHHLAESFLFLPQVSPMDSGPWGCILTYRDGFNVSIMYNLTVLGL
EPPTPLTVYAGAGSRVGLPCRLPAGVGTRSFLTAKWTPPGGGPDLLVTGDNGDFTLRLED
VSQAQAGTYTCHIHLQEQQLNATVTLAIITVTPKSFGSPGSLGKLLCEVTPVSGQERFVW
SSLDTPSQRSFSGPWLEAQEAQLLSQPWQCQLYQGERLLGAAVYFTEL

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	7

Primary citation

LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition. Ming, Q., Celias, D.P., Wu, C. et al. Nat Immunol (2022) 23:1031-1041. DOI 10.1038/s41590-022-01238-7 · PubMed

Other PDB entries of the same protein (UniProt P18627 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7UM3 2.4 Å, Crystal structure of a Fab in complex with a peptide derived from the LAG-3 D1 domain…
7TZH 2.43 Å, Structure of human LAG3 domains 3-4 in complex with antibody single chain-variable…
9BF9 3.4 Å, Human LAG-3-HLA-DR1 complex
8SR0 3.53 Å, CryoEM structure of a therapeutic antibody (favezelimab) bound to human LAG3 local refined
8SO3 3.61 Å, CryoEM structure of a therapeutic antibody (favezelimab) bound to human LAG3

Browse structure collections

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