3G7V: PDB entry 3G7V

Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein. Determined by X-ray diffraction at 1.86 Å resolution. Released 23 Jun 2009.

Method: X-ray diffraction
Resolution: 1.86 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 4
Atoms: 13,356
Mol. weight: 181.04 kDa
Released: 23 Jun 2009

Explore 3G7V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G7V contains 108 α-helices and 97 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: 27 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	6-10	5	1
α-helix	17-31	15
β-strand	34-38	5	1
α-helix	43-51	9
β-strand	59-63	5	1
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	2
α-helix	77-78	2
β-strand	79	1	3
α-helix	83-86	4
β-strand	89	1	4
α-helix	91-95	5
β-strand	98-99	2	3
β-strand	102-103	2	3
β-strand	106-111	6	1
β-strand	114-118	5	5
β-strand	128	1	6
α-helix	129-131	3
α-helix	132-140	9
β-strand	145-147	3	5
α-helix	154-163	10
β-strand	167-172	6	7
β-strand	175-182	8	7
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	5
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	5
α-helix	246-248	3
β-strand	249	1	6
β-strand	250	1	8
β-strand	253	1	8
α-helix	257	1
β-strand	258-259	2	9
β-strand	260-266	7	1
β-strand	267	1	2
α-helix	273-278	6
α-helix	279-284	6
α-helix	287-296	10
β-strand	301-302	2	1
β-strand	304	1	4
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	9
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-368	12
α-helix	378-388	11
α-helix	390-397	8

Chain B: 27 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-10	4	10
α-helix	17-31	15
β-strand	35-38	4	10
α-helix	43-51	9
β-strand	59-63	5	10
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	11
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	12
α-helix	91-95	5
β-strand	98-99	2	13
β-strand	102-103	2	13
β-strand	106-111	6	10
β-strand	114-118	5	14
β-strand	128	1	15
α-helix	129-131	3
α-helix	132-140	9
β-strand	145-147	3	14
α-helix	154-163	10
β-strand	167-172	6	16
β-strand	175-182	8	16
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	14
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	14
α-helix	246-248	3
β-strand	249	1	15
β-strand	250	1	17
β-strand	253	1	17
α-helix	257	1
β-strand	258-259	2	18
β-strand	260-266	7	10
β-strand	267	1	11
α-helix	273-278	6
α-helix	279-284	6
α-helix	287-296	10
β-strand	301-302	2	10
β-strand	304	1	12
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	18
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12
α-helix	378-386	9
α-helix	390-397	8

Chain C: 28 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-10	4	19
α-helix	17-31	15
β-strand	35-38	4	19
α-helix	43-51	9
β-strand	59-63	5	19
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	20
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	21
α-helix	91-95	5
β-strand	98-99	2	22
β-strand	102-103	2	22
β-strand	106-111	6	19
β-strand	114-118	5	23
β-strand	128	1	24
α-helix	129-131	3
α-helix	132-140	9
β-strand	145-147	3	23
α-helix	154-163	10
β-strand	167-172	6	25
β-strand	175-182	8	25
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	23
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	23
α-helix	246-248	3
β-strand	249	1	24
β-strand	250	1	26
β-strand	253	1	26
α-helix	257	1
β-strand	258-259	2	27
β-strand	260-266	7	19
β-strand	267	1	20
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	19
β-strand	304	1	21
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	27
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-368	12
α-helix	375-377	3
α-helix	378-387	10
α-helix	390-394	5

Chain D: 26 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-10	4	28
α-helix	17-31	15
β-strand	35-38	4	28
α-helix	43-51	9
β-strand	59-63	5	28
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	29
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	30
α-helix	91-96	6
β-strand	98-99	2	31
β-strand	102-103	2	31
β-strand	106-111	6	28
β-strand	114-118	5	32
β-strand	128	1	33
α-helix	132-140	9
β-strand	145-147	3	32
α-helix	154-163	10
β-strand	167-172	6	34
β-strand	175-182	8	34
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	32
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	32
α-helix	246-248	3
β-strand	249	1	33
β-strand	250	1	35
β-strand	253	1	35
α-helix	257	1
β-strand	258-259	2	36
β-strand	260-266	7	28
β-strand	267	1	29
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	28
β-strand	304	1	30
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	36
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-368	12
α-helix	378-387	10
α-helix	390-394	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein	A, B, C, D	protein	408	Escherichia coli, Homo sapiens	P0AEX9 (AlphaFold model), P10997 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3G7V_1 Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein (chains A, B, C, D)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNAAAKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Primary citation

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Wiltzius, J.J., Sievers, S.A., Sawaya, M.R. et al. Protein Sci (2009) 18:1521-1530. DOI 10.1002/pro.145 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

Browse structure collections

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