9NAB: Alpha5beta1 integrin headpiece with OS2966 Fab

Cryo-EM structure of the alpha5beta1 integrin headpiece with OS2966 Fab. Determined by electron microscopy at 2.54 Å resolution. Released 23 Jul 2025.

Method: Electron microscopy
Resolution: 2.54 Å
Organisms: Homo sapiens, Mus musculus
Chains: 4
Atoms: 8,498
Mol. weight: 178.58 kDa
Released: 23 Jul 2025

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

Secondary structure: helices and β-sheets

9NAB contains 28 α-helices and 103 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: 16 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	89	1	1
α-helix	93-96	4
β-strand	114-115	2	2
β-strand	118-119	2	1
β-strand	129-132	4	3
β-strand	134-136	3	2
β-strand	143-150	8	4
α-helix	153-155	3
α-helix	156-163	8
α-helix	166-173	8
β-strand	180-187	8	4
α-helix	200-204	5
β-strand	214	1	5
α-helix	215-216	2
β-strand	220-226	7	4
α-helix	229-238	10
α-helix	239-241	3
β-strand	242	1	5
β-strand	249	1	6
α-helix	252-260	9
α-helix	262-265	4
β-strand	271-278	8	4
β-strand	282	1	6
α-helix	287-289	3
β-strand	304	1	7
β-strand	307	1	7
α-helix	315-318	4
α-helix	319-328	10
β-strand	331-338	8	4
α-helix	342-351	10
β-strand	358-360	3	4
α-helix	367-379	13
β-strand	384-385	2	8
β-strand	395-396	2	3
β-strand	399-400	2	9
α-helix	402-404	3
β-strand	406	1	9
β-strand	423-424	2	2
β-strand	425-426	2	9
β-strand	427-430	4	3
β-strand	442-445	4	1
β-strand	446-447	2	8
β-strand	454-457	4	1

Chain B: 8 helices, 40 β-strands

Element	Residues	Length	Sheet
β-strand	50-51	2	10
β-strand	78-80	3	11
β-strand	95-97	3	11
β-strand	120	1	12
β-strand	133	1	12
β-strand	135-136	2	13
β-strand	145	1	14
β-strand	148-149	2	14
β-strand	152-157	6	14
β-strand	161-162	2	13
β-strand	171-172	2	13
β-strand	175-180	6	14
β-strand	185-189	5	14
β-strand	210-213	4	15
β-strand	219-223	5	15
α-helix	226-229	4
β-strand	231	1	16
β-strand	232-236	5	15
α-helix	238-243	6
α-helix	260-262	3
α-helix	265-267	3
β-strand	272	1	16
β-strand	276-279	4	17
α-helix	287	1
β-strand	288-293	6	17
α-helix	296-299	4
β-strand	302-306	5	17
β-strand	315	1	17
β-strand	318	1	17
β-strand	329-333	5	18
β-strand	342-347	6	18
β-strand	353	1	19
β-strand	359	1	19
β-strand	364-368	5	18
β-strand	370-371	2	20
β-strand	374-375	2	20
β-strand	381-384	4	18
β-strand	397-400	4	21
β-strand	409-413	5	21
β-strand	425-427	3	21
α-helix	428-429	2
β-strand	430-431	2	22
β-strand	434-435	2	22
β-strand	441-443	3	21
α-helix	448-449	2
β-strand	459-462	4	10
β-strand	474-478	5	10
β-strand	483-487	5	10

Chain C: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	35	1	30
β-strand	38-39	2	31
β-strand	47-50	4	30
β-strand	61-66	6	31
β-strand	73-77	5	31
β-strand	81-82	2	31
β-strand	90-95	6	30
β-strand	98-103	6	30
α-helix	108-110	3
β-strand	113-118	6	31
β-strand	126	1	31
β-strand	130-132	3	31
β-strand	161-165	5	32
α-helix	192-195	4
β-strand	202-206	5	32

Chain D: 2 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	22-25	4	23
α-helix	26-27	2
β-strand	30-31	2	24
β-strand	38-39	2	23
β-strand	41-44	4	23
β-strand	53-58	6	25
β-strand	65-70	6	25
β-strand	78-79	2	25
β-strand	87-92	6	23
β-strand	97-102	6	23
α-helix	107-109	3
β-strand	111-118	8	25
β-strand	121	1	26
β-strand	124	1	26
β-strand	127-130	4	25
β-strand	134-136	3	25
β-strand	137-138	2	24
β-strand	144	1	27
β-strand	147-148	2	28
β-strand	168-172	5	28
β-strand	173	1	27
β-strand	196-197	2	28
β-strand	203-206	4	28
β-strand	222-225	4	29
β-strand	234-237	4	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Integrin beta-1	A	protein	498	Homo sapiens	P05556 (AlphaFold model)
Human Integrin alpha 5	B	protein	694	Homo sapiens
IgG heavy chain	D	protein	230	Mus musculus
IgG light chain	C	protein	214	Mus musculus

Sequence of entity 1 (A), FASTA

>9NAB_1 Integrin beta-1 (chains A)
QTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDI
ENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAED
YPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTP
AKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAV
CGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIA
HLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSS
EVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDS
DSFKIRPLGFTEEVEVILQYICECEGGLENLYFQGGKNAQCKKKLQALKKKNAQLKWKLQ
ALKKKLAQGGHHHHHHHH

Sequence of entity 2 (B), FASTA

>9NAB_2 Human Integrin alpha 5 (chains B)
FNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPW
GASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYS
WRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVL
GGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEF
SGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLD
DLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGD
LDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALR
GGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVA
CINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAR
EDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQI
LLDCGEDNICVPDLQLEVFGEQNGGLENLYFQGGENAQCEKELQALEKENAQLEWELQAL
EKELAQWSHPQFEKGGGSGGGSGGSAWSHPQFEK

Sequence of entity 3 (D), FASTA

>9NAB_3 IgG heavy chain (chains D)
EVQLQQSGPEVGRPGSSVKISCKASGYTFTGYILSWVKQSPGQGLEWIGWVDPEYGSTDS
AEKFKKRATLTADISSNTAYIQLSSLTSEDTATYFCTRYYDGYYRRWFAYWGQGTLVTVS
SASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTKTYICNVNHKPSNTKVDKKVEPKYGPPCPPC

Sequence of entity 4 (C), FASTA

>9NAB_4 IgG light chain (chains C)
DIQMTQSPASLSASLGDIVSIECLASEGISNNLAWHQQKPGKSPQLLIYGAHSLHDGVPS
RFSGSGSGTQYSLKISGMQPEDEGVYYCQQGYKYPITFGGGTKLELKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Primary citation

ITGB1 Regulates Triple-Negative Breast Cancer Development by Modulating the Tumor Microenvironment. Song, N., Chen, S., Wang, L. et al. Adv Sci (Weinh) (2026) 13:e13672-e13672. DOI 10.1002/advs.202513672 · PubMed

Other PDB entries of the same protein (UniProt P05556 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4WK0 1.78 Å, Metal Ion and Ligand Binding of Integrin
4WJK 1.85 Å, Metal Ion and Ligand Binding of Integrin
3G9W 2.17 Å, Crystal Structure of Talin2 F2-F3 in Complex with the Integrin Beta1D Cytoplasmic Tail
3T9K 2.3 Å, Crystal Structure of ACAP1 C-portion mutant S554D fused with integrin beta1 peptide
8W30 2.45 Å, Crystal structure of alpha-V beta-1 integrin headpiece in complex with TR01225179
4WK2 2.5 Å, Metal Ion and Ligand Binding of Integrin
4WK4 2.5 Å, Metal Ion and Ligand Binding of Integrin
9B9J 2.6 Å, Integrin alpha-5 beta-1 in complex with BIIG2 Fab
9P6S 2.61 Å, Cryo-EM structure of human integrin alpha5beta1 in complex with fibronectin (FN 7-10)
9B9K 2.7 Å, Integrin alpha-5 beta-1 in complex with MINT1526A Fab
7CEB 2.89 Å, Crystal structure of alpha6beta1 integrin headpiece
3VI3 2.9 Å, Crystal structure of alpha5beta1 integrin headpiece (ligand-free form)

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