Brand  (β version)

PDB ID: 2RSE

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Ligands
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TB Terbium(III) ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2RSE   PDBj   RCSB PDB   PDBe
Header : ISOMERASE/TRANSFERASE
Title : NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS
Release Data : 2012-05-30
Compound :
mol_id molecule chains synonym
1 Peptidyl-prolyl cis-trans isomerase FKBP1A A PPIase FKBP1A, 12 kDa FK506-binding protein, 12 kDa FKBP, FKBP-12, FK506-binding protein 1A, FKBP-1A, Immunophilin FKBP12, Rotamase
ec: 5.2.1.8
mol_id molecule chains synonym
2 Serine/threonine-protein kinase mTOR B FK506-binding protein 12-rapamycin complex-associated protein 1, FKBP12-rapamycin complex-associated protein, Mammalian target of rapamycin, mTOR, Mechanistic target of rapamycin, Rapamycin and FKBP12 target 1, Rapamycin target protein 1
ec: 2.7.11.1
fragment: UNP RESIDUES 2019-2112
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: FKBP1A, FKBP1, FKBP12
expression_system_vector: pGBHPS
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1
expression_system_vector: pGBHPS
Authors : Kobashigawa, Y., Ushio, M., Saio, T., Inagaki, F.
Keywords : FKBP12, rapamycin, FK506, lanthanide, PCS, ISOMERASE-TRANSFERASE complex
Exp. method : SOLUTION NMR
Citation :

Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.

Kobashigawa, Y.,Saio, T.,Ushio, M.  et al.
(2012)  J.Biomol.Nmr  53 : 53 - 63

PubMed: 22487935
DOI: 10.1007/s10858-012-9623-8

Reaction

Chain : A
UniProt : P62942 (FKB1A_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0) 5.2.1.8 PubMed:1696686, PubMed:1701173
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Chain : B
UniProt : P42345 (MTOR_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) 2.7.11.1 PubMed:12087098, PubMed:12150925, PubMed:12231510, PubMed:15268862, PubMed:15467718, PubMed:15718470, PubMed:17517883, PubMed:18372248, PubMed:18925875, PubMed:20022946, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:29150432
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) 2.7.11.1 PubMed:12087098, PubMed:12150925, PubMed:12231510, PubMed:15268862, PubMed:15467718, PubMed:15718470, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:29150432, PubMed:29236692, PubMed:37751742
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+) 2.7.10.2 PubMed:26584640
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