1MRK: Alpha-trichosanthin

Name: PDB 1MRK: Studies on crystal structures active center geometry and depurine mechanism of two ribosome-inactivating proteins
Published: 1995-02-07
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ribosome-inactivating protein

Studies on crystal structures active center geometry and depurine mechanism of two ribosome-inactivating proteins. Determined by X-ray diffraction at 1.6 Å resolution. Released 7 Feb 1995.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Trichosanthes kirilowii
Chains: 1
Atoms: 2,067
Mol. weight: 27.43 kDa
Ligands: FMC
Released: 7 Feb 1995

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

Secondary structure: helices and β-sheets

1MRK contains 13 α-helices and 17 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, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
α-helix	11-23	13
β-strand	27-31	5	2
β-strand	34-35	2	2
β-strand	36	1	3
β-strand	37	1	2
α-helix	38	1
α-helix	43-46	4
β-strand	47-53	7	1
β-strand	59-65	7	1
β-strand	70-76	7	1
β-strand	79-82	4	1
α-helix	86-91	6
β-strand	101-104	4	1
α-helix	111-118	8
α-helix	122-124	3
β-strand	127	1	4
α-helix	129-140	12
α-helix	144-155	12
α-helix	156-160	5
α-helix	161-163	3
β-strand	164	1	5
α-helix	165-172	8
β-strand	179	1	4
α-helix	183-202	20
β-strand	208-216	9	6
β-strand	222-227	6	6
α-helix	231-235	5
β-strand	237	1	5
β-strand	240	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-trichosanthin	A	protein	247	Trichosanthes kirilowii	P09989 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MRK_1 ALPHA-TRICHOSANTHIN (chains A)
DVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADETI
SVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAGK
IRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSEAARYKFIEQQIGKRVDKTFL
PSLAIISLENSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALL
LNRNNMA

Ligands and cofactors

ID	Name	Formula	Copies
FMC	(1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol	C10 H13 N5 O4	1

Primary citation

Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins. Huang, Q., Liu, S., Tang, Y. et al. Biochem J (1995) 309:285-298. PubMed

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

1MRJ 1.6 Å, Studies on crystal structures active center geometry and depurine mechanism of two…
1GIS 1.7 Å, A trichosanthin(tcs) MUTANT(E85Q) complex structure with…
1TCS 1.7 Å, Crystal structure of trichosanthin-NADPH complex at 1.7 Å resolution reveals active-site…
1GIU 1.8 Å, A trichosanthin(tcs) MUTANT(E85R) complex structure with adenine
1QD2 1.86 Å, Crystal structure of the complex of trichosanthin with adenine, obtained from…
1NLI 1.93 Å, Complex of [E160A-E189A] trichosanthin and adenine
1J4G 2.0 Å, crystal structure analysis of the trichosanthin delta C7
2JDL 2.2 Å, Structure of C-terminal region of acidic P2 ribosomal protein complexed with trichosanthin
2JJR 2.3 Å, V232K, N236D-trichosanthin
2VS6 2.4 Å, K173A, R174A, K177A-trichosanthin

Browse structure collections

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