1RQQ: Insulin Receptor Kinase

Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of APS. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Dec 2003.

Method
X-ray diffraction
Resolution
2.6 Å
Organisms
Homo sapiens, Rattus norvegicus
Chains
6
Atoms
6,300
Mol. weight
101 kDa
Ligands
MN, 112
Released
30 Dec 2003

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

Secondary structure: helices and β-sheets

1RQQ contains 46 α-helices and 40 β-strands across 6 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.

Chains A and B: 18 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand99011
β-strand996-1005101
β-strand1008-101691
β-strand1024-103071
α-helix1038-105114
β-strand105912
α-helix1060-10612
β-strand1062-106651
α-helix10721
β-strand1073-107751
β-strand108312
α-helix1084-10907
α-helix1104-11052
α-helix1106-112520
β-strand1128-112923
α-helix1135-11373
β-strand1138-114032
β-strand1146-114832
β-strand1155-115623
β-strand1163-116424
β-strand1169-117135
α-helix1173-11753
α-helix1178-11836
β-strand1185-118624
α-helix1188-120316
α-helix1207-12082
α-helix1215-12239
α-helix1228-12314
α-helix1236-124510
α-helix1250-12523
α-helix1254-12552
α-helix1256-12638
α-helix1271-12744
Chains C and D: 4 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix404-4063
β-strand410111
α-helix416-4249
α-helix427-4304
β-strand434-438511
β-strand446-452711
β-strand455-461711
α-helix470-48415
Chains E and F: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix105-1073
β-strand109-11135

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Insulin receptorA, Bprotein306Homo sapiensP06213 (AlphaFold model)
adaptor protein APSC, Dprotein114Rattus norvegicusQ9Z200 (AlphaFold model)
Bisubstrate inhibitorE, Fprotein18
Sequence of entity 1 (A, B), FASTA
>1RQQ_1 Insulin receptor (chains A, B)
VFPSSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESAS
LRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAEN
NPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDI
YETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQ
VLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPNMRPTFLEIVNLLKDDLHPSFPEVSFF
HSEENK
Sequence of entity 2 (C, D), FASTA
>1RQQ_2 adaptor protein APS (chains C, D)
GSHMELELSDYPWFHGTLSRVKAAQLVLAGGPRSHGLFVIRQSETRPGECVLTFNFQGKA
KHLRLSLNGHGQCHVQHLWFQSVFDMLRHFHTHPIPLESGGSADITLRSYVRAQ
Sequence of entity 3 (E, F), FASTA
>1RQQ_3 BISUBSTRATE INHIBITOR (chains E, F)
KKKLPATGDFMNMSPVGD

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn2
112Thiophosphoric acid O-((adenosyl-phospho)phospho)-S-acetamidyl-diesterC12 H19 N6 O13 P3 S2

Primary citation

Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Hu, J., Liu, J., Ghirlando, R. et al. Mol Cell (2003) 12:1379-1389. DOI 10.1016/S1097-2765(03)00487-8 · PubMed

Other PDB entries of the same protein (UniProt P06213 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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