9PWN: Fabs 7411

Crystal structure of Fabs 7411 in complex with TREM2 peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 10 Sept 2025.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,629
Mol. weight: 49.9 kDa
Released: 10 Sept 2025

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

Secondary structure: helices and β-sheets

9PWN contains 17 α-helices and 44 β-strands across 2 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 H: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	10-12	3	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	33-39	7	2
β-strand	45-51	7	2
β-strand	58-60	3	2
β-strand	65	1	1
β-strand	68-73	6	1
α-helix	74-76	3
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-99	8	2
β-strand	111-112	2	2
β-strand	116-120	5	2
α-helix	123-125	3
β-strand	126	1	3
α-helix	127-128	2
β-strand	129-133	5	4
β-strand	144-154	11	4
β-strand	155	1	3
β-strand	160-163	4	5
α-helix	164-166	3
β-strand	168	1	5
β-strand	172-174	3	4
α-helix	175-177	3
β-strand	178-179	2	4
β-strand	185-194	10	4
α-helix	195-197	3
β-strand	204-209	6	5
α-helix	210-212	3
β-strand	214-219	6	5

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	6
β-strand	10-13	4	7
β-strand	19-25	7	6
β-strand	33-38	6	7
β-strand	45-49	5	7
β-strand	53-54	2	7
α-helix	55	1
β-strand	62-67	6	6
β-strand	70-75	6	6
α-helix	80-82	3
β-strand	84-90	7	7
α-helix	96	1
β-strand	97-98	2	7
β-strand	102-106	5	7
β-strand	111	1	8
α-helix	112-113	2
β-strand	114-118	5	9
α-helix	119-121	3
α-helix	122-127	6
β-strand	129-139	11	9
β-strand	140	1	8
β-strand	144-150	7	10
β-strand	153-154	2	10
β-strand	159-163	5	9
α-helix	164-167	4
β-strand	173-182	10	9
α-helix	183-187	5
β-strand	191-198	8	10
β-strand	205-210	6	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
7411 Fab Heavy Chain	H	protein	221	Homo sapiens
7411 Fab Light Chain	L	protein	212	Homo sapiens
TREM-2 stalk peptide	A	protein	18	Homo sapiens	Q9NZC2 (AlphaFold model)

Sequence of entity 1 (H), FASTA

>9PWN_1 7411 Fab Heavy Chain (chains H)
EVQLLESGGGLVQPGGSLRLSCAASGFTFSERAMTWVRQAPGKGLEWVSSISGSGVKTYY
ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKTPSPKYVGSVFDLWGRGTLVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVE

Sequence of entity 2 (L), FASTA

>9PWN_2 7411 Fab Light Chain (chains L)
DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPS
RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPYTFGQGTKLEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRG

Sequence of entity 3 (A), FASTA

>9PWN_3 TREM-2 stalk peptide (chains A)
DPLDHRDAGDLWFPGESE

Primary citation

Building a potent TREM2 agonistic, biparatopic, common light chain antibody. da Silva Almeida, A., Geddie, M.L., Bhate, A. et al. MAbs (2025) 17:2546554-2546554. DOI 10.1080/19420862.2025.2546554 · PubMed

Other PDB entries of the same protein (UniProt Q9NZC2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
5UD8 1.8 Å, Crystal Structure of Mutant Ig-like Domain
8T51 1.9 Å, Crystal structure of Fab 3.10C2 bound to TREM2
8T59 2.0 Å, Crystal structure of Para.09 bound to TREM2
6B8O 2.2 Å, WT Ig-like V Domain with Phosphatidylserine
5UD7 2.2 Å, Crystal Structure of Wild-Type Ig-like Domain
6Y6C 2.26 Å, TREM2 extracellular domain (19-174) in complex with single-chain variable fragment…
6YMQ 3.07 Å, TREM2 extracellular domain (19-131) in complex with single-chain variable 4 (scFv-4)
5ELI 3.1 Å, Triggering receptor expressed on myeloid cells 2
6YYE 3.36 Å, TREM2 extracellular domain (19-131) in complex with single-chain variable fragment…
9PX5 3.7 Å, Crystal structure of Fab 7268 in complex with MBP-TREM2 Ig domain fusion
6Z0G Structure of TREM2 transmembrane helix in DPC micelles

Browse structure collections

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