1IGR: Type 1 Insulin-like growth factor receptor

Type 1 Insulin-like growth factor receptor (DOMAINS 1-3). Determined by X-ray diffraction at 2.6 Å resolution. Released 27 Sept 1999.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,900
Mol. weight: 57.07 kDa
Ligands: NAG
Released: 27 Sept 1999

Explore 1IGR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1IGR contains 13 α-helices and 40 β-strands across 1 chain. 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: 13 helices, 40 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
β-strand	7-10	4	2
α-helix	13-19	7
β-strand	24-25	2	1
β-strand	29-35	7	2
β-strand	50-51	2	1
β-strand	55-61	7	2
α-helix	66-68	3
β-strand	75-76	2	1
β-strand	82	1	2
β-strand	85-90	6	2
β-strand	105-106	2	1
β-strand	110-114	5	2
α-helix	127-130	4
α-helix	134-136	3
β-strand	138-140	3	2
α-helix	145-148	4
β-strand	164-166	3	3
β-strand	171-173	3	3
β-strand	175	1	4
β-strand	181	1	4
α-helix	182-183	2
α-helix	187-189	3
β-strand	194	1	5
β-strand	200	1	5
β-strand	205-209	5	6
β-strand	218-221	4	6
β-strand	224-225	2	7
β-strand	230-231	2	7
β-strand	239-241	3	7
β-strand	245-247	3	7
α-helix	249-253	5
β-strand	267-269	3	7
β-strand	272-274	3	7
β-strand	281-283	3	8
β-strand	291-293	3	8
α-helix	298-299	2
β-strand	301-311	11	9
α-helix	315-317	3
β-strand	325-332	8	9
α-helix	345-348	4
β-strand	353-354	2	9
β-strand	358-361	4	9
β-strand	377-378	2	9
β-strand	384	1	9
β-strand	388-393	6	9
β-strand	410-411	2	9
β-strand	415-419	5	9
β-strand	421	1	10
α-helix	426-436	11
β-strand	447	1	9
β-strand	452	1	10
α-helix	474-477	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Insulin-like growth factor receptor 1	A	protein	478	Homo sapiens	P08069 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1IGR_1 INSULIN-LIKE GROWTH FACTOR RECEPTOR 1 (chains A)
EICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRV
AGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLC
YLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNR
CQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYR
FEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPK
VCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKI
RHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAF
NPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVDDDDKEQKLISEEDLN

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2

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

Primary citation

Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. Garrett, T.P., McKern, N.M., Lou, M. et al. Nature (1998) 394:395-399. DOI 10.1038/28668 · PubMed

Other PDB entries of the same protein (UniProt P08069 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1P4O 1.5 Å, Structure of Apo unactivated IGF-1R KInase domain at 1.5A resolution.
8PYN 1.71 Å, Human IGF1R with inhibitor 56
3LW0 1.79 Å, IGF-1RK in complex with ligand MSC1609119A-1
5FXS 1.9 Å, IGFR-1R complex with a pyrimidine inhibitor.
2OJ9 2.0 Å, Structure of IGF-1R kinase domain complexed with a benzimidazole inhibitor
3I81 2.08 Å, Crystal structure of insulin-like growth factor 1 receptor (IGF-1R-WT) complex with…
1JQH 2.1 Å, IGF-1 receptor kinase domain
1K3A 2.1 Å, Structure of the Insulin-like Growth Factor 1 Receptor Kinase
3O23 2.1 Å, Human unphosphorylated IGF1-R Kinase domain in complex with an hydantoin inhibitor
4D2R 2.1 Å, Human IGF in complex with a Dyrk1B inhibitor
3NW7 2.11 Å, Crystal structure of insulin-like growth factor 1 receptor (IGF-1R-WT) complex with a…
3NW5 2.14 Å, Crystal structure of insulin-like growth factor 1 receptor (IGF-1R-WT) complex with a…

Browse structure collections

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