4ARZ: Gtr1p-Gtr2p

The crystal structure of Gtr1p-Gtr2p complexed with GTP-GDP. Determined by X-ray diffraction at 3.1 Å resolution. Released 25 Jul 2012.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
2
Atoms
4,870
Mol. weight
75.52 kDa
Ligands
GTP, MG, GDP
Released
25 Jul 2012

Explore 4ARZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ARZ contains 24 α-helices and 23 β-strands across 2 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: 11 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand6-1381
α-helix19-279
α-helix33-386
α-helix40-423
β-strand44-5181
β-strand55-6281
α-helix66-738
α-helix77-804
β-strand86-9271
α-helix98-11518
β-strand120-12671
α-helix133-15321
β-strand160-16451
α-helix170-17910
α-helix187-20014
β-strand204-20962
β-strand215-21952
α-helix242-25413
β-strand264-26962
β-strand273-27752
β-strand282-28762
α-helix295-30814
Chain B: 13 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand813
β-strand13-1754
α-helix22-3211
α-helix34-385
α-helix39-435
α-helix48-503
β-strand5413
β-strand59-6354
α-helix74-829
β-strand85-9174
α-helix97-11317
β-strand118-12474
α-helix131-14616
α-helix148-1514
β-strand159-16354
α-helix170-18213
α-helix184-1863
α-helix188-1969
β-strand202-20982
β-strand217-21822
α-helix228-24518
β-strand270-27562
β-strand280-28562
β-strand290-29672
α-helix303-32422

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding protein GTR1Aprotein310SACCHAROMYCES CEREVISIAEQ00582 (AlphaFold model)
GTP-binding protein GTR2Bprotein341SACCHAROMYCES CEREVISIAEP53290 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4ARZ_1 GTP-BINDING PROTEIN GTR1 (chains A)
MSSNNRKKLLLMGRSGSGKSSMRSIIFSNYSAFDTRRLGATIDVEHSHLRFLGNMTLNLW
DCGGQDVFMENYFTKQKDHIFQMVQVLIHVFDVESTEVLKDIEIFAKALKQLRKYSPDAK
IFVLLHKMDLVQLDKREELFQIMMKNLSETSSEFGFPNLIGFPTSIWDESLYKAWSQIVC
SLIPNMSNHQSNLKKFKEIMNALEIILFERTTFLVICSSNGENSNENHDSSDNNNVLLDP
KRFEKISNIMKNFKQSCTKLKSGFKTLILNNNIYVSELSSNMVCFIVLKDMNIPQELVLE
NIKKAKEFFQ
Sequence of entity 2 (B), FASTA
>4ARZ_2 GTP-BINDING PROTEIN GTR2 (chains B)
MSLEATDSKAMVLLMGVRRCGKSSICKVVFHNMQPLDTLYLESTSNPSLEHFSTLIDLAV
MELPGQLNYFEPSYDSERLFKSVGALVYVIDSQDEYINAITNLAMIIEYAYKVNPSINIE
VLIHKVDGLSEDFKVDAQRDIMQRTGEELLELGLDGVQVSFYLTSIFDHSIYEAFSRIVQ
KLIPELSFLENMLDNLIQHSKIEKAFLFDVNSKIYVSTDSNPVDIQMYEVCSEFIDVTID
LFDLYKAPVLRNSQKSSDKDNVINPRNELQNVSQLANGVIIYLRQMIRGLALVAIIRPNG
TDMESCLTVADYNIDIFKKGLEDIWANARASQAKNSIEDDV

Ligands and cofactors

IDNameFormulaCopies
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg1
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

Crystal Structure of the Gtr1Pgtp-Gtr2Pgdp Complex Reveals Large Structural Rearrangements Triggered by GTP-to-Gdp Conversion. Jeong, J.H., Lee, K.H., Kim, Y.M. et al. J Biol Chem (2012) 287:29648. DOI 10.1074/JBC.C112.384420 · PubMed

Other PDB entries of the same protein (UniProt Q00582 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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