5FFG: Integrin alpha V beta 6 head

Crystal structure of integrin alpha V beta 6 head. Determined by X-ray diffraction at 2.25 Å resolution. Released 25 Jan 2017.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Homo sapiens
Chains: 2
Atoms: 7,099
Mol. weight: 100.09 kDa
Ligands: NAG, CA
Released: 25 Jan 2017

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

Secondary structure: helices and β-sheets

5FFG contains 29 α-helices and 68 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 A: 14 helices, 55 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
β-strand	9-12	4	2
β-strand	22-26	5	3
β-strand	35-40	6	3
β-strand	55-60	6	3
β-strand	67-70	4	3
α-helix	77-78	2
β-strand	79-81	3	4
β-strand	84-85	2	4
β-strand	87-88	2	5
β-strand	97-101	5	6
β-strand	104-109	6	6
β-strand	113-114	2	5
β-strand	123	1	5
β-strand	127-132	6	6
β-strand	135-139	5	6
β-strand	160-163	4	7
β-strand	168-173	6	7
α-helix	176-179	4
β-strand	181	1	8
β-strand	182-187	6	7
α-helix	188-193	6
β-strand	208-209	2	7
α-helix	210-212	3
α-helix	215-217	3
β-strand	222	1	8
β-strand	225-229	5	9
α-helix	237	1
β-strand	238-243	6	9
α-helix	246-249	4
β-strand	252-256	5	9
β-strand	263-268	6	9
β-strand	279-283	5	10
β-strand	292-297	6	10
β-strand	301-303	3	11
β-strand	309-311	3	11
β-strand	314-320	7	10
β-strand	326-332	7	10
β-strand	343-348	6	12
β-strand	357-362	6	12
α-helix	367-369	3
β-strand	372-377	6	12
β-strand	378-379	2	13
β-strand	382-383	2	13
β-strand	389-392	4	12
β-strand	408-413	6	2
β-strand	422-427	6	2
α-helix	428-430	3
β-strand	432-436	5	2
α-helix	437	1
β-strand	438	1	1
α-helix	439-440	2
β-strand	441-442	2	14
β-strand	443-451	9	15
β-strand	454-455	2	16
β-strand	463	1	17
β-strand	470	1	17
β-strand	473-483	11	15
β-strand	491-500	10	18
β-strand	512-514	3	15
β-strand	521-529	9	18
α-helix	533-534	2
β-strand	535-543	9	15
α-helix	544-545	2
α-helix	546-548	3
β-strand	556-564	9	18
β-strand	578-579	2	14
β-strand	586-591	6	18
β-strand	592-593	2	16

Chain B: 15 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	116-123	8	19
α-helix	126-128	3
α-helix	129-134	6
α-helix	135-137	3
α-helix	138-149	12
β-strand	153-160	8	19
α-helix	173-177	5
α-helix	188-190	3
β-strand	193-200	8	19
α-helix	203-212	10
β-strand	223	1	20
α-helix	225-234	10
α-helix	236-239	4
β-strand	246-253	8	19
β-strand	257	1	20
α-helix	260-266	7
β-strand	270	1	21
α-helix	271-272	2
β-strand	278	1	22
β-strand	283	1	19
β-strand	284	1	22
β-strand	290	1	21
α-helix	291-294	4
α-helix	295-304	10
β-strand	307-313	7	19
α-helix	315-327	13
β-strand	332-335	4	19
α-helix	343-354	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Integrin alpha-V	A	protein	601	Homo sapiens	P06756 (AlphaFold model)
Integrin beta-6	B	protein	257	Homo sapiens	P18564 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5FFG_1 Integrin alpha-V (chains A)
FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCD
WSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQ
EREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQ
GQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLF
MDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAI
AAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSGCPPSFGYSMKGATDIDKNGY
PDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCL
KADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELI
AYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDTGGL
E

Sequence of entity 2 (B), FASTA

>5FFG_2 Integrin beta-6 (chains B)
TEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVK
TTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIM
QAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVCPNDGLCHLDSKNEYSMSTVL
EYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISA
YEELRSEVELEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
CA	Calcium ion	Ca	6

Water and common crystallization additives (SO4, PEG, MES) are not listed.

Primary citation

Force interacts with macromolecular structure in activation of TGF-beta. Dong, X., Zhao, B., Iacob, R.E. et al. Nature (2017) 542:55-59. DOI 10.1038/nature21035 · PubMed

Other PDB entries of the same protein (UniProt P06756 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9CZD 2.23 Å, Crystal structure of integrin avb6 headpiece in complex with compound 30
8W30 2.45 Å, Crystal structure of alpha-V beta-1 integrin headpiece in complex with TR01225179
9CZA 2.49 Å, Crystal structure of integrin avb6 headpiece in complex with compound 18
4UM9 2.5 Å, Crystal structure of alpha V beta 6 with peptide
9CZF 2.53 Å, Crystal structure of integrin avb6 headpiece in complex with compound MORF-627
9CZ7 2.57 Å, Crystal structure of integrin avb6 headpiece in complex with compound 12
6OM1 2.66 Å, Crystal structure of an atypical integrin
8VS6 2.73 Å, L-TGF-b3/avb8
6OM2 2.77 Å, Crystal structure of atypical integrin alphaV beta8 with proTGF-beta1 ligand peptide
9IUJ 2.78 Å, Integrin alpha-v beta-3 in complex with rhodostomin
9LT3 2.79 Å, Integrin alpha-v beta-3 in complex with Trimucrin
8XEL 2.8 Å, Cryo-EM structure of integrin ITGAV/ITGB3 complex, conformation 3

Browse structure collections

About this viewer

MolViewer shows 5FFG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.