1GIS: PDB entry 1GIS

A trichosanthin(tcs) MUTANT(E85Q) complex structure with 2'-deoxy-adenosin-5'-monophosphate. Determined by X-ray diffraction at 1.7 Å resolution. Released 3 Jun 2003.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Trichosanthes kirilowii
Chains
1
Atoms
2,276
Mol. weight
27.63 kDa
Ligands
D5M
Released
3 Jun 2003

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

Secondary structure: helices and β-sheets

1GIS contains 16 α-helices and 15 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: 16 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand3-641
α-helix12-2514
β-strand28-3252
β-strand35-3842
α-helix391
α-helix44-474
β-strand48-5471
β-strand60-6671
β-strand71-7771
β-strand80-8341
α-helix87-926
β-strand102-10541
α-helix1061
α-helix112-1198
α-helix123-1253
β-strand12813
α-helix130-14112
α-helix148-1569
α-helix157-1615
α-helix162-1643
β-strand16514
α-helix166-1738
β-strand18013
α-helix181-1833
α-helix184-20421
β-strand209-21795
β-strand223-22865
α-helix232-2365
β-strand23814
β-strand24112
α-helix244-2463

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribosome-inactivating protein alpha-trichosanthinAprotein248Trichosanthes kirilowiiP09989 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1GIS_1 RIBOSOME-INACTIVATING PROTEIN ALPHA-TRICHOSANTHIN (chains A)
MDVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADET
ISVAIDVTNVYIMGYRAGDTSYFFNQASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAG
KIRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSEAARYKFIEQQIGKRVDKTF
LPSLAIISLENSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIAL
LLNRNNMA

Ligands and cofactors

IDNameFormulaCopies
D5M2'-deoxyadenosine-5'-monophosphateC10 H14 N5 O6 P1

Primary citation

Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants. Guo, Q., Zhou, W., Too, H.M. et al. Protein Eng (2003) 16:391-396. DOI 10.1093/protein/gzg056 · PubMed

Other PDB entries of the same protein (UniProt P09989 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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