2G48: Human insulin-degrading enzyme

crystal structure of human insulin-degrading enzyme in complex with amylin. Determined by X-ray diffraction at 2.6 Å resolution. Released 24 Oct 2006.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 16,709
Mol. weight: 237.43 kDa
Ligands: DIO
Released: 24 Oct 2006

Explore 2G48 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2G48 contains 119 α-helices and 72 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: 59 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	47-50	4	1
β-strand	63-69	7	1
β-strand	74-79	6	1
β-strand	85-92	8	1
α-helix	96-98	3
α-helix	106-113	8
α-helix	114-116	3
β-strand	118	1	2
α-helix	126-132	7
β-strand	137-142	6	1
β-strand	147-154	8	1
α-helix	155-157	3
α-helix	158-166	9
α-helix	167-169	3
β-strand	172	1	2
α-helix	176-193	18
α-helix	197-208	12
α-helix	214-216	3
α-helix	223	1
α-helix	224-228	5
α-helix	229-232	4
α-helix	237-248	12
α-helix	251-253	3
β-strand	254-260	7	1
α-helix	264-275	12
α-helix	283-286	4
α-helix	295-297	3
β-strand	300-304	5	3
β-strand	312-319	8	3
α-helix	323-325	3
α-helix	330-338	9
α-helix	346-352	7
β-strand	359-367	9	3
β-strand	370-378	9	3
α-helix	381-384	4
α-helix	387-404	18
α-helix	408-423	16
α-helix	425-429	5
α-helix	430-440	11
α-helix	446-448	3
α-helix	461-468	8
α-helix	473-475	3
β-strand	477-481	5	3
α-helix	483-485	3
β-strand	491-492	2	3
β-strand	499-504	6	3
α-helix	505-506	2
α-helix	507-514	8
α-helix	536-539	4
β-strand	549-553	5	4
β-strand	557-563	7	4
β-strand	571-579	9	4
α-helix	581-583	3
α-helix	587-613	27
β-strand	616-623	8	4
β-strand	626-634	9	4
α-helix	638-650	13
α-helix	656-671	16
α-helix	672-675	4
α-helix	678-690	13
β-strand	691	1	5
α-helix	697-703	7
α-helix	709-721	13
β-strand	722-723	2	6
β-strand	724-731	8	4
α-helix	735-753	19
β-strand	756-757	2	6
α-helix	758-759	2
α-helix	760-762	3
β-strand	768	1	5
β-strand	769	1	7
α-helix	771-772	2
β-strand	775-782	8	8
β-strand	789-799	11	8
α-helix	802-820	19
α-helix	821-826	6
β-strand	832-840	9	8
β-strand	843-852	10	8
α-helix	856-876	21
α-helix	879-894	16
α-helix	895-897	3
α-helix	900-912	13
α-helix	920-928	9
α-helix	933-939	7
α-helix	940-944	5
β-strand	952-959	8	8
α-helix	981-985	5
α-helix	988-989	2
β-strand	990-991	2	8
α-helix	992	1
α-helix	995-1000	6
β-strand	1004	1	7
α-helix	1007-1012	6

Chain B: 59 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	47-51	5	9
β-strand	63-69	7	9
β-strand	74-79	6	9
β-strand	85-92	8	9
α-helix	96-98	3
α-helix	106-113	8
β-strand	118	1	10
α-helix	126-132	7
β-strand	137-142	6	9
β-strand	147-154	8	9
α-helix	158-166	9
α-helix	167-169	3
β-strand	172	1	10
α-helix	176-194	19
α-helix	197-206	10
α-helix	214-216	3
α-helix	223	1
α-helix	224-228	5
α-helix	229-232	4
α-helix	237-248	12
α-helix	251-253	3
β-strand	254-260	7	9
α-helix	264-275	12
α-helix	283-286	4
α-helix	295-297	3
β-strand	300-304	5	11
β-strand	312-320	9	11
α-helix	323-325	3
α-helix	330-338	9
α-helix	346-352	7
β-strand	356-367	12	11
β-strand	370-379	10	11
α-helix	387-404	18
α-helix	408-424	17
α-helix	425-429	5
α-helix	430-440	11
α-helix	446-448	3
α-helix	461-468	8
α-helix	473-475	3
β-strand	477-481	5	11
α-helix	483-485	3
β-strand	491-492	2	11
β-strand	499-504	6	11
α-helix	505-506	2
α-helix	507-514	8
α-helix	524-527	4
α-helix	538-541	4
β-strand	549-553	5	12
β-strand	557-563	7	12
β-strand	571-579	9	12
α-helix	581-583	3
α-helix	587-613	27
β-strand	616-622	7	12
β-strand	626-634	9	12
α-helix	638-650	13
α-helix	656-671	16
α-helix	672-675	4
α-helix	678-690	13
β-strand	691	1	13
α-helix	697-702	6
α-helix	703-706	4
α-helix	709-721	13
β-strand	722-723	2	14
β-strand	724-731	8	12
α-helix	735-753	19
β-strand	756-757	2	14
α-helix	758-759	2
α-helix	760-762	3
α-helix	766-767	2
β-strand	768	1	13
β-strand	769	1	7
α-helix	771-772	2
β-strand	775-782	8	15
β-strand	789-799	11	15
α-helix	802-820	19
α-helix	821-826	6
β-strand	832-840	9	15
β-strand	843-852	10	15
α-helix	856-875	20
α-helix	879-894	16
α-helix	895-897	3
α-helix	900-912	13
α-helix	920-928	9
α-helix	933-939	7
α-helix	940-944	5
β-strand	952-959	8	15
α-helix	981-986	6
α-helix	988-989	2
β-strand	990-991	2	15
α-helix	992	1
α-helix	995-1000	6
β-strand	1004	1	7
α-helix	1007-1012	6

Chain C: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	3
α-helix	3-5	3
β-strand	14-15	2	1

Chain D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	11
β-strand	14-15	2	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Insulin-degrading enzyme	A, B	protein	990	Homo sapiens	P14735 (AlphaFold model)
Islet amyloid polypeptide	C, D	protein	37		P10997 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2G48_1 Insulin-degrading enzyme (chains A, B)
MHHHHHHAAGIPMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAA
LDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNY
YFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATG
NPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTN
LVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSN
PGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVED
IILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEV
LTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEV
IKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFL
PKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYL
SVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLL
MTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTL
IEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLE
LFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLIT
MEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLK
TLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQP
EVIQNMTEFKRGLPLFPLVKPHINFMAAKL

Sequence of entity 2 (C, D), FASTA

>2G48_2 Islet amyloid polypeptide (chains C, D)
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Ligands and cofactors

ID	Name	Formula	Copies
DIO	1,4-diethylene dioxide	C4 H8 O2	2

Primary citation

Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Shen, Y., Joachimiak, A., Rosner, M.R. et al. Nature (2006) 443:870-874. DOI 10.1038/nature05143 · PubMed

Other PDB entries of the same protein (UniProt P14735 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3CWW 1.96 Å, Crystal Structure of IDE-bradykinin complex
2G47 2.1 Å, Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-40)
2G56 2.2 Å, crystal structure of human insulin-degrading enzyme in complex with insulin B chain
4PES 2.21 Å, Crystal structure of insulin degrading enzyme complexed with inhibitor tert-butyl…
4PFC 2.21 Å, Crystal structure of insulin degrading enzyme complexed with inhibitor
2G54 2.25 Å, Crystal structure of Zn-bound human insulin-degrading enzyme in complex with insulin B…
3E4Z 2.28 Å, Crystal structure of human insulin degrading enzyme in complex with insulin-like growth…
3E50 2.3 Å, Crystal structure of human insulin degrading enzyme in complex with transforming growth…
4PF7 2.33 Å, Crystal structure of insulin degrading enzyme complexed with inhibitor
3OFI 2.35 Å, Crystal structure of human insulin-degrading enzyme in complex with ubiquitin
2G49 2.5 Å, Crystal structure of human insulin-degrading enzyme in complex with glucagon
4PF9 2.5 Å, Crystal structure of insulin degrading enzyme complexed with inhibitor

Browse structure collections

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